Amino acids exchange obtained from CKD patients via Exome Sequencing differ radically from those of natural variants 1000 genome and genomAD databases

Amino acids exchange obtained from CKD patients via Exome Sequencing differ radically from those of natural variants 1000 genome and genomAD databases | Research Square window.SnipcartSettings = { analytics: { enabled: false } }; (function() { var accessVector = localStorage.getItem('access_vector') || ''; window.dataLayer = window.dataLayer || []; if (accessVector) { window.dataLayer.push({ user: { profile: { profileInfo: { snid: accessVector } } } }); } })(); (function(w,d,s,l,i){w[l]=w[l]||[];w[l].push({'gtm.start':new Date().getTime(),event:'gtm.js'});var f=d.getElementsByTagName(s)[0],j=d.createElement(s),dl=l!='dataLayer'?'&l='+l:'';j.async=true;j.src='https://www.googletagmanager.com/gtm.js?id='+i+dl;f.parentNode.insertBefore(j,f);})(window,document,'script','dataLayer','GTM-K279D39R'); Browse Preprints In Review Journals COVID-19 Preprints AJE Video Bytes Research Tools Research Promotion AJE Professional Editing AJE Rubriq About Preprint Platform In Review Editorial Policies Our Team Advisory Board Help Center Sign In Submit a Preprint Cite Share Download PDF Research Article Amino acids exchange obtained from CKD patients via Exome Sequencing differ radically from those of natural variants 1000 genome and genomAD databases Edem Nuglozeh, Mohammad Feroze Fazaludeen, Fatih Sağlam This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-4268762/v1 This work is licensed under a CC BY 4.0 License Status: Posted Version 1 posted You are reading this latest preprint version Abstract Background: Nonsynonymous mutations in the coding regions of human genes are responsible for phenotypic differences between humans and for their susceptibility to genetic disease. Methods: We performed Exome sequencing on CKD patients’ genomic DNA and put the focus in understanding the role played by the amino-acid mutation spectrum (PAM) in human chronic kidney disease CKD patients. More specifically, using SIFT algorithm, we generated the amino acids substitution on proteins and compared the PAM matrix derived from CKD patients representing the amino-acid mutational spectrum to non-disease PAM matrices representing spectra of mutual amino-acid mutation frequencies derived from 1000 genome and genomAD database. Results: We found a strong and positive correlation in term of mutabilities of amino acids distribution in human proteome and the average distribution of amino acid mutability remains higher in genomAD dataset as compared CKD and 1000 genome. The results also show a strong correlation of mutability between the three datasets, the coefficient of correlation being: ( r CKD vs 1kg = 0.9225 , r CKD vs genomAD = 0.943 1 and r genomAD vs 1kg = 0.9486 ) as well probabilistic distribution of amino acids in human proteome between the three datasets. Conclusion: The amino acids mutability index in CKD dataset was statistically different as compared with those in 1000 genome and genomAD datasets. There is strong positive correlation in mutabilities of amino acids distribution in human proteome and the average distribution of mutability is higher in genomAD dataset as compared CKD and 1000 genome. In the CKD dataset, Arginine remains a common product of mutability from four amino acids like: Tryptophan, Histidine, Glycine and Lysine and the spike of Arginine in blood samples should be an element to trace in diagnostic profile of CKD. The data paved a way for clinical use for amino acids exchanges in chronic kidney disease using Illumina platform. CKD PAM Matrix Amino Acids Mutability Figures Figure 1 Figure 2 Figure 3 Figure 4 Figure 5 Figure 6 1. Background DNA is an adaptable and dynamic molecule. As such, the nucleotides residing inside the DNA molecule undergo through multiple permutations under an evolutional process called mutation and this process spans the entire human genome. Some of these mutations can be harmless, beneficial or deleterious to human being according to the nature of the mutation. We are invariably trained under the paradigm that all biological activities in cells are embedded in three letters code that fall under the denomination as genetic codes. The change in genetic code has long been seen as the main vectors of genetic diseases and these diseases ignite as the hurtful mutations or deleterious mutations that take over the biological system. These mutations have direct impact on amino acids sequences and it was shown that the disease-causing variants usually provoke drastic changes of amino acid physico-chemical properties of proteins such as charge, hydrophobicity and geometry arrangement [1]. Variants involved in diseases tend to cause more changes of hydrogen bond network and salt bridges as compared with harmless amino acid mutations [2,3]. Diseases-associated variants target the more conserved sequences in genome that relatively remained unchanged far back in the phylogenic tree as observed in 1 kG database [4]. However, most of phenotypical effects and molecular cause of origin of most variants remain elusive so anticipating or predicting a single amino acid change in a specific disease will be of great medical interest. Genetic variants underlying common disease may vary in frequency across population more than random variants do in the genome, perhaps because of their exposition to epigenetics events due to natural selection [5]. The Next-generation sequencing (NGS) is instrumental in the discovery of growing number of novel candidate’s genes variants and most importantly rare variants in pharmacogenes [6]. The 1000 Genomes Project was developed to serve as a big repertoire and global reference for human genetic variation and is used to serve as a baseline for subsequent research in establishing the relationship between genotype and phenotype and ultimately identifying the genetic basis of human disease [7]. Basically, the 1 kG database serves as a reference where researchers can vet multiple SNPs resulting from exome and genome sequencing. Besides the 1kG database, the genome aggregation database or genomAD was also developed with the goal of accumulating and harmonizing both exome and genome sequencing data from a wide variety of large-scale sequencing projects. The most recent data set (gnomAD v2.1) provides access to more than 125,000 exome and 15,000 whole-genome sequences from unrelated and healthy adults sequenced as part of various disease-specific and population genetic studies. It has accumulated 15708 whole genome and 125748 of exomes. Its predecessor, the Exome Aggregation Consortium (ExAC) has been mentioned in more than 4,000 publications [8]. The genomAD includes the genomes and exomes from European, Latino African, African American, South East Asian, Ashkenazi Jewish and other population. The gnomAD papers reported 241 million small genetic variants (single nucleotide variants and short insertion/deletion variants) and 335,470 structural variants (DNA rearrangements of at least 50 base pairs), compared with 7.4 million small genetic variants identified in (ExAC). Recently, the gnomAD team is already expanding the resource further and has recently released gnomAD v3, which contains 71,702 genomes. The Genome Aggregation Database (gnomAD) has paved the road to reveal the spectrum of mutational constraints affecting human protein-coding genes in a catalog predicting loss-of-function variants in 125,748 whole-exome and 15,708 whole-genome sequencing datasets [8], analysis and prediction loss-of-function variants from 125,748 human exomes and 15,708 whole genomes. It also provides a roadmap for human ‘knockout’ studies into disease biology and drug-target selection [4] and large empirical assessment that provides a reference map for disease-association studies, population genetics, and diagnostic screening [9]. One way of discovering the function of a gene is to study what happens when the gene is disrupted by a mutation. These variants often have adverse outcomes and are usually rare. Large genetic sequencing studies provide an opportunity to examine the effects of these loss-of-function variants, which could provide important insights into human biology and diseases [10]. With the existence of myriad of variants datasets, the establishment of novel disease-datasets becomes promising. It was in this optic that we began the study of chronic kidney failure disease (CKD) with hope to establish a nsSNPs for this disease. Chronic kidney disease (CKD) is a major global health problem and affects approximately one in ten adults worldwide [11]. Both genomic and environmental factors contribute to this complex heterogeneous disease. CKD heritability is estimated to be high (30–75%). Although the estimation of Mendelian disorders is supposed to be responsible for 10% of ESRD cases [12], 15%–30% of patients, including those with presumably acquired forms of disease such as diabetic or hypertensive nephropathy, report a family history of renal disease. This indicates the existence of a contribution of hereditary factors across clinical categories [13]. Moreover, affected individuals within the same family frequently carry different clinical diagnoses or spectrum, suggesting that they may be sharing genetic contributions across CKD subtypes [13] and recent studies support this hypothesis [14]. For example, two variants in APOL1 (Online Mendelian Inheritance in Man reference number [OMIM]: 603743) significantly increase the risk for multiple forms of CKD, including focal segmental glomerulosclerosis (FSGS), hypertension-attributed nephropathy, and HIV-1–associated nephropathy [15]. In similar way, mutations in the type-4 collagen genes ( COL4A3 [OMIM: 120070], COL4A4 [OMIM: 120131], and COL4A5 [OMIM: 303630]) traditionally associated with Alport syndrome can also manifest frequently as FSGS [16]. Collectively, these findings highlight the potential of an in depth of genetic and sequencing studies to identify the shared causative variants spanning all the spectrum of CKD and ultimately undertake clinical studies to uproot the basis of underlying molecular pathophysiological causes of CDK. To address some part of this issue, we conducted exome sequencing on gDNA of 12 young patients suffering of kidney failure. After bioinformatics analysis of our exome sequencing data, more than 250 SNPs per sample were retained as variants of interest. Combined harder filtrations are operated on these presumptive SNPs which narrowed them down to two single SNPs (data not shown) as these results will be reported separately in another publication aimed at addressing the functionality of those genes. Recently, we also reported and published karyotyping and chromosome HeatMap of some regional genomic of interest from the same CKD patients [17]. Here we sought to establish and describe the relationship between PAM matrices obtained from these CDK patients that we separately established and compared them to 1000 genome and genomAD dataset matrices thus allowing us to derive and compare the combined mutability of each amino acids derived from CDK patients as well as the amino acids from the two datasets, 1kG and genomAD. These measures allow us to establish the ranking mutabilities of the amino acids among the three data sets as well as a profile of amino acids mutations that can be damageable in disease situation like CKD. 2. Methods 2.1. Objective This study has four specific objectives: 1 . To sequence the human genome from patients suffering from chronic kidney disease, on Illumina-MiSeq platform. 2 . Exploring the possibilities of correlation between plasma and urinary kidney profile and some biochemical parameters, as well of association between known phenotypic SNPs and amino acids exchange. 3 . Investigating the existence of deleterious amino acids exchange. 4 . Authenticating these exchanges on phenotypic basis by reconstructing the variant genes harboring these mutations paving the way for future development of animal models for ex vivo 2.2. Genomic DNA library preparation and sequencing High quality gDNA was purified from lymphocytes whole as described elsewhere. The construction of the library was conducted using the Nextera Rapid Capture kits (Illumina) 50 ng of gDNA was utilized using transposase-based chemistry to create exome libraries Library was Qc on Bioanalyzer 2100, (Agilent Technology, Santa Clara, CA) to assess the integrity and size library fragments 2 x 75 paired end cycles were performed (+1 cycle to each forward and reverse read to allow for phasing/pre-phasing). 2.3. Bioinformatics analyses The flow chart for bioinformatics analysis have been published by our team elsewhere. Below are summarized successive steps we used in bioinformatics analysis. a. Read Trimming and Clipping of Adapters Reads are trimmed from the 3' end to have at least a phred score of 30 . Illumina sequencing adapters are removed from the reads, and all reads are required to have a length of at least 50 bp. Trimming and clipping are performed using Trimmomatic(Bolger, Lohse, and Usadel 2014) [18]. This step generated: Samples Readset, Raw pair Read, number of Paired Reads obtained from the sequencer, the number of Remaining Paired Reads after the trimming step and the percentage of Surviving Paired Reads and Raw Paired Reads. b. Read Alignment to a Reference Genome The filtered reads are aligned to a reference genome. The genome used in this analysis is Homo_sapiens assembly hg19 . Each readset is aligned using BAW [Li and Durbin (2010)] [19] which creates a Binary Alignment Map file (bam). Then we merged all readset BAM files from the same sample into a single global BAM file using Picard . BWA is a fast light-weighted tool which aligns relatively short sequences (queries) to a sequence database (target), such as the human reference genome. It is based on the Burrows-Wheeler Transform (BWT). BWA is designed for short queries up to ~200 bp with low error rate (< 3%). It does gap global alignment, supports paired-end reads, and is one of the fastest short read alignment algorithms to date while also visiting suboptimal hits. c. Read Alignment Improvement Because of lack of perfect aligner tool, the alignment step remains really sensitive to the aligner parameters as well as technical and biological variations. To increase the quality and speed of subsequent variant calling, we performed a series of procedures to improve the alignment. These procedures consist of realigning the surrounding short insertions or deletions, fixing possible read mate discrepancy due to realignment marking duplicated reads and recalibrating read base quality. d. Realigning Short Insertions and Deletions (INDELs) The realignment is done using GATK (DePristo et al. 2011) [20]. INDELs in reads (especially near the ends) can trick the mappers into mis-aligning with mismatches. These artifacts resulting from mismatches can harm base quality recalibration and variant detection. Realignment around INDELs helps to improve the accuracy of several downstream steps. Insertion and deletion realignment is performed on regions where multiple base mismatches are preferred over INDELs by the aligner since it appears to be less costly for the algorithm. Such regions will introduce false positive variant calls which may be filtered out by realigning those regions properly. Mainly realignment will occur in 3 different region types: (1) Known sites (e.g., dbSNP, 1000 Genomes), (2) INDELs seen in original alignments (in CIGARs) (3) Sites where evidence suggests a hidden INDEL. e. Fixing Read Mates Once local regions are realigned, the read mate coordinates of the aligned reads need to be recalculated since the reads are realigned at positions that differ from their original alignment. The read mate positions fixing is performed using multi-task application Picard and will be subsequently used to mark duplicates . f. Marking Duplicates Because Exome Sequencing experiment encompasses several PCR amplifications steps which could induce coverage bias during the library construction, this bias could generate high level of false positives and false negatives during the variant calling steps (SNV, SV and CNV). Thus, removing or marking read duplicates using Picard is an important step of the sequencing analysis. Aligned reads are duplicates if they have the same 5' alignment positions (for both mates in the case of paired-end reads). All but the best pair (based on alignment score) will be marked as a duplicate in the bam file. Duplicates reads will be excluded in the subsequent analysis. g. Base Quality Recalibration This step allows recalibrating base quality scores of sequencing-by-syntheses reads in an aligned BAM file. After recalibration, the quality scores in the QUAL field in each read in the BAM output are more accurate in that, the reported quality score is closer to its actual probability of mismatching to the reference genome. QUAL represents the accuracy of the genotyping and when QUAL is 20, this means that there is 99% probability that there is a variant at the site. The recalibration process is accomplished by analyzing the covariation among several features of a base. For example: (1) Reported quality score, (2) the position within the read and (3) the preceding and current nucleotide (sequencing chemistry effect) observed by the sequencing machine. These covariates are then subsequently applied through a piecewise tabular correction to recalibrate the quality scores of all reads in a BAM file. The recalibration process is performed using GATK (DePristo et al. 2011) [20] h. Sequencing and Alignment Metrics per Sample The aim of this step is to provide each sample a general summary statistics and Sample readsets are merged for clarity. i. SNV Annotations An in-house database identifies regions in which reads are confidently mapped to the reference genome. Generally, low mappability corresponds to RepeatMasker regions and decreases substantially with the increasing in the read length. A region is identified as HC = coverage too high, LC = low coverage, MQ = too low mean mapQ (< 20) and ND = unmappable region (no data) at the position. The VCF files are also annotated for: dbSNP using the SnpSift software (Cingolani, Patel, et al. 2012) [21]. Variant effects (predicted variant effects on gene, such as amino acid changes) using the SnpEff software (Cingolani, Platts, et al. 2012) [21]. The SnpSift http://snpeff.sourceforge.net/SnpSift.html software which is a toolbox used to filter and localize missense which are number of variants in coding region for which the variation generates a codon modification. This lead to generate two types of variant metrics tables: variants for codons changes and amino acids changes induced by SNV. j. Variants Metrics The variant metrics and statistics have been generated using the SnpEff software (Cingolani, Platts, et al. 2012) [21]. The variant metrics and statistics have been generated using the SnpEff software (Cingolani, Platts, et al. 2012) [21]. 2.4. Non-synonymous mutations in humans We query two reference data sets for natural human variants that we used work. The first set of natural variants was from the 1000 Genomes Project (1kG), and the second from gnomAD. The 1kG data comprises a compilation of human DNA variants from 1092 individuals from diverse populations across the world. Only variants with a frequency of occurrence of >1% were included. To avoid the presence of unstable elements, major histocompatibility and immunoglobulin were removed from group of the transcripts. Of interest here were the variants that mapped to protein coding regions as synonymous (sSNPs) and non-synonymous (nsSNPs) variants. These were obtained from Ensembl [22] v67, as described in de Beer et al [1]. The other source of natural variants was gnomAD, which contains data from various disease-specific and population genetic studies. We used v.2.0 which had variants from over 140,000 individuals. The data were downloaded from the Broad Institute’s web site. As with the 1kG data, the genome coordinates had to be converted to the corresponding sSNPs and nsSNPs in the relevant protein coding regions to get the amino acid changes involved. 2.5. Non-synonymous mutations in humans from CKD Patients As initially reported in section bioinformatics analysis, each transcript representative for each protein sequence obtained from the VCF files was allocated Ensembl ID using the mapping tool provided by Uniprot. We derived nsSNPs for each protein from CKD from VCF files using SnpEff software and the metrics converted into two tables with one representing codon change and the other one amino acids exchange with each record of entry on Y-axis symbolized by one single letter amino acid. Because, major histocompatibility complex and immunoglobulins are inherently unstable, they were removed from the pool of the transcripts The data set representative of amino acids exchanges is later converted into amino acid pair score matrices or exchange frequencies among amino acids. 2.6. Statistical Analysis We calculated the Pearson correlation coefficient (r P ) to examine the linear relationship between the variables and the Spearman correlation coefficient (r S ) to examine the monotonous relationship over sequence numbers. We interpreted the obtained correlations data as strong relationship if 0.7 < |r| ≤ 1, as moderate relationship when 0.4 < |r| ≤ 0.7, and for weak or absence of relationship if 0 ≤ |r| ≤ 0.4. We analyzed the differences in the mutation numbers between the Patients, 1kg on one hand the patients and gnomAD datasets using Fisher's exact test. We applied Bonferroni correction to the p-values when examining multiple comparisons. We obtained all analysis results and graphics using the R package program (R Core Team, 2021) [23]. We will have weak correlation, if 0 ≤ |r| ≤ 0.4, moderate correlation, if 0.4 < |r| ≤ 0.7 and strong correlation if 0.7 < |r| ≤ 1 3. Results This project was carried out to compare the amino acids exchange from CKD patients databases compared to the amino acids exchanges from 1000 genome and genomAD databases. The data from CKD patients were obtained by carrying out exome sequencing on genomic DNA libraries built from the patients genomic DNA (see methods). We already published the biochemical profiles from these patients in Eur. J. Med. Health. Sci [17}. The Average distribution of capture sub regions from exome sequencing is presented on Fig 1. This distribution of mutation sites within genomic regions from different variants in CKD patients is distributed to nine genomic regions. This statistical repartition of the variants may represent a transition bias observed in introns, pseudogenes, and other noncoding regions (Gojobori et al. 1983;) [24] The biochemical pipelines and ANOVAR tool we used for the bioinformatic analysis of the FASTQ data are presented were published elsewhere [17]. These were instrumental in experimental determination nsSNPs which were filtered and annotated with respect to their functions. In Fig 2, we presented the codons HeatMap changes in CKD patients. The codons exchange frequencies in the transcripts reflect the cumulative distribution of codons mutability for silent (blue area), missense (yellow spots) nonsense (red spots) and this distribution of mutability itself depends on the absence or presence CpG dinucleotides islands. The inset colors show the probability density distribution by the type of mutation. The variation in colors reflect the degree of exchanges: blue color signifies low exchanges whereas red color is associated with high exchanges. In table 1, we presented the amino acids exchanges in CKD patients, together with the amino acids’ exchanges derived from the 1000 genome and genomAD databases. We carried out the exome sequencing project in patients with CKD in part to retrieve all nsSNPs and their associated transcripts. These SNPs were submitted to successive bioinformatic analysis and underwent through many steps of hard filtering (see method) to ascertain that, just all pathological SNPs of interest were retained from which we produced a square matrice 20x20 of amino acids substitution from CKD patients. We also simultaneous carried out analysis of amino acids exchange matrix generated from 1091 individuals obtained from 1000 genome dataset and 140,000 individuals from genomAD database. The CKD matrix combined with the 1 kg matrix and the genomAD matrix presented in table 1 depicted an asymmetric configuration in term of topology which itself is inherent to the difference in mutability of different codons and the pathological state of different proteins in CKD samples [25, 26]. This difference in mutability is due in part by flanking nucleotides context of the mutation site. Indeed, it has been reported that up one heptamers, 3 nucleotides upstream and 3 nucleotides downstream of the site of nsSNPs, can affect the mutation [27-30]. For example, the elevation in mutation rate is due to methyl cytosine deamination at CpG dinucleotides [31] and more specifically, mutability stemming from nonsynonymous mutations depends on the specificality of the amino acids that are exchanged, reflecting differences in both physicochemical properties [32] and metabolic effects [33]. 3.1. Mutability of amino acids in CKD, 1000 genome and genomAD Matrix The mutability of the amino acids in the three databases are summarized on table 1. Each cell contains information about each amino acid from the three databases, with on the top, the CKD, in the middle the 1 kg and genomAD in the bottom and the subsequent presentation of the rest of our results in this table will follow this order. Talking about the mutability of the amino acids among the three databases, Arginine remains the most mutable amino acid all tree databases with the mutability metrics organized respectively from the top to the bottom in its cell is (0.022, 0.030 and 0.021) for the three databases. Inside the cell, Arginine mutability from 1000 genome dataset remains higher vis a vis to Arginine mutability in CKD database which itself is higher than Arginine mutability in genomAD dataset. However, those amino acids with more chemical complexity structures like: Tryptophan and Phenylalanine respectively depict the lowest mutabilities values for the three datasets (CKD, 1 kg and genomAD) with Tryptophan mutability being (0.007, 0.004 and 0.006) respectively for the three databases and Phenylalanine mutability being (0.005, 0.004 and 0.006) respectively. We also compared the probabilistic distribution of amino acids in human proteome between the three datasets (see figure S1 ). On Y axis is shown the number of mutations of amino acids and on X axis we presented the frequency of occurrence of the amino acids in human proteome. From this result, it is clear that Arginine and Leucine represent the outliers in that they deviate from the common alignment on the axe from other amino acids. The result also shows moderate correlation between the mutability and the probabilistic distribution of the amino acids in human proteome in the three datasets with their correlation coefficients being: ( r CKD = 0.6062, r 1kg = 0.4808, r genomAD = 0.6430 ). The same moderate positive correlation is also observed in ( figure S2 ). The analysis of data from 1 kg dataset presents the relationship between mutabilities and the number of codons with the correlation coefficient being ( r 1kg = 0.4334 ) whereas data from CKD and genomAD datasets show week correlation with the correlation coefficients representing the relation between their mutabilities and their number of codons being ( r CKD = 0.3108, r genomAD = 0.2852 ) respectively. Contrarily to moderate and weak correlation values observed between the number of codons and their mutabilities on one hand, on the other hand, the comparison of mutabilities between the three datasets presented on fig 3 shows strong correlation with their respective correlation coefficient comparison being: (r CKD vs 1kg =0.9225 , r CKD vs genomAD = 0.9431 and r genomAD vs 1kg = 0.9486). This is a clear demonstration that, on the evolutionary basis, the distance between proteins from the three datasets is close since it is generally accepted that more substitutions of amnio acids are needed to change one evolutionary sequence into another one and the more substitutions we have, the larger becomes the evolutionary distance [34]. Besides, the evolutionary property also depends on some amino acid properties like isoelectric point, polarity and volume [35]. The close evolution distance between the three databases as observed on fig 3 is also reiterated on (figure S3 ) where we show strong correlation between the mutability and the number of mutations at least in CKD and 1 kg datasets and moderate correlation in genomAD database, with 1000 genome dataset being (r 1000 genome = 0.8702), followed by CKD patients (r CKD = 0.7002) moderate correlation in genomAD dataset (r genomAD = 0.6442). The figure S4 compares the number of mutations to the natural occurrence of amino acids in human proteome and the three databases depicted moderate correlation between the number of mutations and the natural occurrence of amino acids. Indeed, it was reported that variability in mutation is context-depend [36-38], and it is well known that, the prediction of mutation variability rate in the human genome is linked to the environment surrounding the sites of mutation [36-38]. Voight and Aggarwala [36] reported from the variant site that, three nucleotides upstream positions and downstream positions surrounding the site of the mutation affect the mutation, which means that up to 7-mer sequence context is detrimental for the mutation to take place. 3.2. Nature of amino acids exchange in CKD, 1000 genome and genomAD databases The profile of one single amino acid changing to all other 19 amino acids in human proteome in all three datasets is portrayed on fig 4 and this is depicted as % of change one amino acid to all other amino acids and the frequency of the occurrence of different exchanges is clearly depicted between different amino acids. For example, in the CKD patient’s dataset, more mutations are recorded for: Tryptophan ( W ), Histidine ( H ), Glycine ( G ) and Lysine ( K ) and these four later four amino acids have Arginine as an end product in term of mutability (p<0.0001) and both Methionine ( M ) and Isoleucine ( I ) being mostly changed into valine ( V ) (p<0.0001). We should recall that ( M and I ) are hydrophobic amino acids with aliphatic chain. In the concept of exchangeability, ( I ) which is hydrophobic aliphatic amino acid will preferably be substituted by another hydrophobic amino acid, particularly aliphatic amino acids and this assertion is true for M too [39]. On the structural basis, being hydrophobic, ( I ) prefers to be buried in hydrophobic protein cores besides being Cβ-branched like ( V ) and Threonine ( T ). Then, in substrates recognition and hydrophobic ligands binding basis, (I) and M can easily be substituted to V [39]. The amino acid substitutions in diseases have well been documented [40]. Amino acids share common properties and several classifications has been adopted and sometimes, it is difficult to put all amino acids of the same group into a one invariant group because, each amino acid in a different protein environment will have different characteristics and one cannot a priori determine its role in the protein based on hydrophobicity or polarity and no-polarity nature. On large scale of naturally occurring of human amino acid variations, it was demonstrated that there is a preference for some amino acid substitutions to be associated with diseases as it is frequently observed for the Arginine [40]. The other way of classifying amino acids is the use of mutation substitution (PAM) matrix. High value in this matrix is indicative that substitution often seen in nature is favorable and vice versa . Mutation matrices are used as a rough guide for how good or bad a particular change will be. Another useful aspect of this concept is that, the matrix can be calculated for different datasets, most especially in diseases situation. We have generated the mutation (PAM) matrix for CKD and came up with particular specific features in amino acids changes characterizing four amino specific acids: Tryptophan ( W ), Histidine ( H ), Glycine ( G ) and Lysine ( K ) all together changing to Arginine ( R ) and this confirmed previous past observation with Arginine ( R ) being frequently associated with diseases states [40]. Tryptophan ( W ) is an aromatic amino acid, but its uniqueness in term of chemistry and size means that its replacement by anything else will be disastrous and we are encountering this the situation in CKD. This drastic situation in term of exchangeability between amino acids of different groups is seen with Histidine ( H ) too which is generally considered to be a polar amino acid, however its uniqueness with regard to its chemical properties makes of ( H) not a particularly good candidate for substitution with any other amino acid. However, ( H ) was also changed to ( R ) which is a positively-charged, polar amino acid. Arginine ( R ) generally prefers to be on the surface of the protein, but its amphipathic nature means that part of the side chain is buried. Lysine ( K ) can be substituted by Arginine ( R ) or other polar amino acids. In the determination of the involvement of ( K ) biological activity in protein function, the substitution of ( K ) with ( R ) completely eliminates the biological activity of TGF-α [41]. 3.3. Amino acid mutability Hierarchy Scores The mutability scores of the amino acids are depicted on fig 5 and among the three databases, the most mutable amino acids remain again the Arginine ( R ). Arginine ( R ) besides of being encoded by six codons, it harbors two CpG units and has thus has higher the potential mutability propensity and targetability as compared to Methionine ( M ) which is coded by one single codon, but still performs well in term of mutability score. 3.4. Distribution of average protein mutabilities for all human proteins in the 1 kG, genomAD and CKD patients The fig 6 presents the average distribution of proteins mutability shows that all amino acids proportionally exhibit higher mutability in genomAD dataset compared to 1 kg and CKD datasets and the average proteins mutability in CKD as well as in 1 kg are equally comparable. This higher mutability in genomAD is inherent to the gene fragments contained in this dataset as it harbors genomic variants as well as transcript variants. Discussion Chronic kidney disease (CKD) is defined as abnormalities in kidney structure or function and requires either GFR below 60 ml/min/1.73 m 2 or markers of kidney damage, including albuminuria [42]. It is a congruence of many vascular diseases with patients having dysfunctions of many physiological pathways. The pathology is infiltrated by other diseases like: diabetes, hypertension [43-45], cardiovascular morbidity [46, 47] as well as many genetic abnormalities like genomic instability [47, 48-51]and instability which is later translated into chromosomal damage and ultimately culminating to renal pathologies. Recent progress in genome-wide association studies revealed SNPs linked to different pathologies associated to CKD like: hypertension [52], coronary artery disease [53], subclinical vascular disease [54] and overlapping between genetic variants observed in CKD patients and cardiovascular pathologies [55]. The goal of our study is to establish a repertoire of allelic variants that are susceptible to kidney diseases and ultimately find some candidate genes directly linked to CKD. To this end, we run exome sequencing from CKD patient samples and determined the average mutation distribution sites within genomic regions from different variants. After bioinformatic analysis coupled with filtrations and hard filtrations, we came up with two single genes that are common to all patients (data not shown as we will be reporting this separately). We also derived the substitutions or exchanges between the amino acids, their mutabilities as well as the probabilistic distribution of these amino acid exchanges in human proteome. Our results from this study provides a unique relation between amino acids exchanges status in CKD. The results as presented on table 1 clearly show a statistically difference between some individual amino acids exchange matrix in CKD patients as compared with the natural variants, we derived from 1000 genome and genomAD datasets. Our data corroborate with those reported by De Beer et al [1] that the amino acids change in disease-associated variants differed radically from variants obtained from 1000 genome dataset. In this study, we went one step forward to establish a net difference in variation between amino acids exchanges deriving from CKD patients to those obtained from 1000 genome and genomAD datasets. This is a first demonstration as such in the scope of CKD patients using a square PAM matrix format 20 X 20 PAM to derive amino acids substitution and their plausible mutabilities in renal disease. In the concept of mutability, it is also known that cytosines in a cytosine–guanine (CpG) dinucleotide context is known for their propensity to mutate at a rate that can be several hundred-fold greater than transversions at other bases , and in genetic variation, these representations are disproportionately represented. It was shown that, hotspots regions of CpG dinucleotides islands play a role in mutational mechanism leading to determination of the amino acids that are prone to mutation. Our data in genomAD in term of mutability presents the same profile as well as the one from 1000 genome dataset as compared with CKD dataset where some cells in our table 1 present statistically significant difference in term of exchangeability between the CKD patients’ dataset. However, the genomAD database shows a proportionally higher mutability for all amino acids compared to 1 kg and CKD datasets and the average proteins mutability in CKD as well as in 1 kg are equally comparable (fig 6). This difference in mutability is inherent to the nature of the three datasets. First, we obtained the CKD dataset from Exome sequencing experiment on Illumina Platform. Then, the DNA sequencing we are dealing with stemmed from the transcripts although some primers from Illumina kits can sometime overlap with some intervening sequences and thereby introducing possibilities that some genomic sequence may be carried on in the results of sequencing data. Second, whereas the1000 genome database was developed using a combination of multiple sequencing approaches, including: low coverage whole genome sequencing, with depth mean of 7.4X, deep Exome sequencing with depth mean of 65.7X and dense microarray genotyping, the result in this database is believed to emanate from the transcript pools uniquely. Therefore, scientists use 1000 genome data base as reference to run variants for Exome sequencing data. Lastly, the genomAD database in contrary was developed by harmonizing both exome and genome sequencing data from a wide variety of large-scale sequencing projects, then it is a direct combination of Exome sequencing and whole genome sequencing data, and this may explain the higher proportion of mutability index score observed in this database comparatively to 1000 genome and CKD datasets. Moreover, on genomic scale, the human genome is known to contain ∼ 30,000 CpG islands , long stretches (CpG repeats) of DNA and with unusually elevated levels of CpG dinucleotides with many occurring at genes promoters. CpG islands are also residents of intervening sequences making the genes prone to mutation thus explaining their contribution to diseases. This also explains a higher distribution of average mutability in genomAD as compared with 1 kg and CKD as seen in fig 6. In our experiment reported in (figure S1), we compared the number of mutations and the probabilistic distribution of amino acids in human proteome. We observed that Arginine (R) was the outlier with higher mutability index as compared to the rest of amino acids. In fine, after the observation of the natural variants in genomAD as well as in 1000 genome databases, it is conclusive to say that the amino acids mutability is mostly driven by the nature and state of the DNA and the mutational mechanisms are favored at the codons harboring the CpG dinucleotides context and this explain why Arginine (R) mutates more than twice than other amino acids. This increase in Arginine (R) variants and mutability we observed in the three datasets can be explained by the deamination of methylated cytosine (5mC) that is changed upon mutation into thymine, which is not readily detected by DNA repair systems. Interestingly, Arginine (R) is the only amino acid to contain CpG dinucleotides at the first and second codon positions, which are less redundant than the third wobble position and therefore more likely to lead to an amino acid change. Moreover, Arginine (R) is encoded by six codons in vertebrate genomes with following features: four CGN codons (CGA, CGC, CGG, CGU) and two AGR codons (AGG, AGA). Base-pair changes in any of these codons can have a wide extensive range of effects in human genome, including: substitution of 12 different amino acids, two stop codons as well as eighteen synonymous mutations. Four amino acids, viz: Tryptophan, Histidine Glutamine and Cysteine account for 75% exchanges for arginine. This implies that the mechanism of selection purification or mutational bias is at work. The transitions of four (A > T and G >A) of six of arginine codons appear to be the drivers behind canonical mutation of arginine codons, a universal signature that independent of the origin of disease tissues. Indeed, recent studies have demonstrated that (A > T and G >A transitions are the causes of depletion of Arginine in human cancers [56]. Then, codon usage four CGN codons despite the hypermutability at CpG dinucleotides islands and the existence of AGR alternative codons, suggests the propensity of negative selective pressure directed toward these sites thereby amounting for the evolution of genetic code through Arginine bias mutation in from our CKD patients. Indeed, data archived in the database of clinically relevant variants (ClinVar) (57) revealed that arginine substitutions underlie 20.0% of all pathogenic single-nucleotide variants (SNVs), making arginine the most commonly substituted amino. The analysis of human genome has found that genes with coding regions of CGN arginine codons are present in higher proportion as compared with AGR arginine codons and CGN codons were enriched among disease genes and with strong correlation with measures of variance intolerance, an indication that, genes with CGN signatures preference are more likely to sustain single-genes mutation diseases (58). Moreover, data from thermodynamic experiments have reported that disease-causing variants have tendency to destabilize protein structures and their interactions [59, 60]. Later on, mutagenesis studies have also reported that replacing nonpolar group by polar ones can increase protein solubility. For example, on the study with RNase Sa, it was found that, the most buried carboxylic groups which are Asp33 (99% buried) and Asp79 (85% buried) and their respective mutants D33A mutants and D79A are 6kcal/mol and 3.3 kcal/mol less stable than the wild type [61, 62] and replacing Thr 76 by Asp acid increase the protein solubility [59]. In our current study, we noticed that four major amino acids, viz : Tryptophan (W), Histidine (H), Glycine (G) and Lysine (L) have Arginine (R) as common final common product of mutability. Whether this phenomenon is specifically peculiar to kidney diseases or widely observed features in biological arena, this remains to be investigated thoroughly via site-specific mutagenesis studies because each amino acid has its profile of physicochemical characteristic property and can therefore influence the final protein chemical structure. Nonetheless, this observation is the first we are reporting in kidney disease. It is also well documented that the determination of protein distances between many sequences necessitates the knowledge of the amino acids substitution rates [26] and invariably, the evolutionary pressure also depends on some amino acid physicochemical properties like isoelectric point, polarity and its volume [27]. We analyzed and compared the amino acids substitution rates between our three datasets and observed a strong positive correlation between the mutabilities as reported on fig 3 and (figure S3 ). This positive correlation demonstrates a close evolutionary distance between the proteins, at least from the three datasets we investigated: our CKD database, 1kg and genomAD database. During evolution, energetically favorable interaction is preserved and intra-protein remaining vicinities depend on the residual amino acids and unfavorable interaction are eliminated. Since it is generally accepted that more substitutions of amnio acids are needed to change one evolutionary sequence into another one and the more substitutions we have, the larger becomes the evolutionary distance [26 27], the substitution data we generated from the three-database correlate with the literature Conclusion We run Exome sequencing and established a PAM matrix of amino acids changes in CKD patients and compared this matrix to matrices obtained from 1000 genome and genomAD databases. The data demonstrated that the amino acids mutability index in CKD data was statistically significant different as compared with 1000 genome and genomAD datasets. There is strong positive correlation in mutabilities of amino acids distribution in human proteome and the average distribution of mutability is higher in genomAD dataset as compared CKD and 1000 genome. In the CKD dataset, Arginine remains a common product of mutability from four amino acids like: Tryptophan, Histidine, Glycine and Lysine and Arginine was shown to be also the outlier and the driver of mutability in the three data sets. More experiments remained to be conducted, more especially using other diseases context dataset to ascertain the peculiar mutability pattern of Arginine. Nonetheless, this study remains the first finding to layout clearly a profile of amino acids changes in CKD as well as a jump in mutability in genomAD dataset. Declarations Ethics approval This study is part of a subgroup of an investigation started while ago on hemodialysis patients from outpatient’s clinics of King Khaled Hospital. The ethic approval committee issued patients’ informed consent for participation authorization for publishing to Dr. Alaraj. [17-]and the subsequent four publications emanating from these patients were under the same authorization Dr. Alaraj who negotiated the blood samples. Availability of data and material CKD patients’ raw data: SNPs files, amino acids exchanges files as well as nucleotides interconversion are the authors property. These databases were generated by the authors for publication. Once they are published, the raw data can be shared with some credible scientists if they make a direct request to the corresponding author. 1000 genome natural variants were obtained from Ensembl [22] v67, as described in de Beer et al [1]. The natural variants from gnomAD dataset (v.2.0) were downloaded from the Broad Institute’s web site. Competing interests Authors declare no competing interests. Fundings Edem Nuglozeh received in part financial support from The University of Hail in Saudi Arabia, and Hail City Kidney foundation. Author contributions All authors contributed to the study conception and design. Material preparation, data collection and analysis were performed by [ Edem Nuglozeh and Mohammad F. Fazaludeen ], [ Fatih Sağlam ] performed the graphic art work, organization of amino acids PAM matrix and statistics analysis. The first draft of the manuscript was written by [ Edem Nuglozeh ] and all authors commented on previous versions of the manuscript. All authors read and approved the final manuscript for publication. 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Epub 2005 Oct 21. PMID: 16288913. et al. Asp79 makes a large, unfavorable contribution to the stability of RNase Sa. J. Mol. Biol. 354 , 967–978 (2005). Tables Table 1. Observation of amino acids exchanges in human proteins variants from To Total MUT R K D E N Q S G H T A P Y V M C L F I W R 709 0 1 2 2349 476 773 2071 137 3 280 0 0 80 1374 371 0 63 1048 9737 0.022 738 0 0 0 4630 553 761 4125 247 0 216 0 0 71 3420 467 0 137 2695 18060 0.030 29213 0 0 0 118098 31134 51256 90111 13721 0 23584 0 0 2910 89234 33386 0 4590 73483 560720 0.021 K 907 0 740 392 238 9 0 0 199 8 4 0 0 51 0 3 2 52 0 2605 0.006 1151 0 843 689 346 0 0 0 300 0 0 0 0 87 0 0 0 84 0 3500 0.006 54592 0 44799 37900 18060 0 0 0 18093 0 0 0 0 5339 0 0 0 4017 0 182800 0.007 D 1 0 793 1006 0 0 551 242 1 181 0 203 162 0 0 2 0 0 0 3142 0.008 0 0 855 1994 0 0 780 419 0 153 0 378 379 0 0 0 0 0 0 4958 0.010 0 0 45423 75306 0 0 43503 25077 0 10473 0 21961 21126 0 0 0 0 0 0 242869 0.011 E 2 1219 890 3 485 0 506 0 0 276 0 0 175 0 0 1 0 0 0 3557 0.006 0 2682 983 0 631 0 628 0 0 319 0 0 241 0 0 0 0 0 0 5484 0.007 0 108957 51791 0 39030 0 39604 0 0 19204 0 0 14615 0 0 0 0 0 0 273201 0.008 N 3 482 560 0 0 1336 1 159 182 0 0 94 0 0 0 0 0 105 0 2922 0.010 0 546 516 0 0 2030 0 236 170 0 0 133 0 0 0 0 0 158 0 3789 0.010 0 32632 26842 0 0 71753 0 12805 10421 0 0 7260 0 0 0 0 0 9553 0 171266 0.010 Q 1262 314 0 354 0 1 0 724 2 0 261 0 0 0 0 140 0 1 0 3059 0.008 875 351 0 521 0 0 0 764 0 0 243 0 0 0 0 192 0 0 0 2946 0.006 49660 16788 0 27915 0 0 0 39814 0 0 16273 0 0 0 0 10064 0 0 0 160514 0.007 S 455 4 4 1 1061 0 781 0 644 468 777 161 2 0 374 669 420 167 49 6037 0.009 648 0 0 0 1103 0 659 0 637 273 541 284 0 0 673 1386 816 242 44 7306 0.008 39566 0 0 0 47105 0 35001 0 33559 15717 30612 13424 0 0 34040 42111 42633 12231 4466 350465 0.009 G 1229 0 633 644 0 0 1226 0 0 495 0 0 451 0 148 1 0 0 55 4882 0.009 1957 0 852 804 0 0 1598 0 0 469 0 0 630 0 197 0 0 0 84 6591 0.009 89095 0 42935 39897 0 0 61049 0 0 31884 0 0 34963 0 13229 0 0 0 6421 319473 0.010 H 925 0 183 0 124 429 0 0 0 2 122 497 0 0 0 91 0 0 0 2373 0.011 863 0 130 0 166 486 0 0 0 0 145 869 0 0 0 188 0 0 0 2847 0.010 44061 0 8282 0 8587 25300 0 0 0 0 10406 37655 0 0 0 9487 0 0 0 143778 0.012 T 208 182 3 0 271 1 667 1 3 1620 312 2 0 1197 0 3 0 1066 0 5536 0.013 206 200 0 0 389 0 740 0 0 1420 186 0 0 2272 0 0 0 1781 0 7194 0.013 12803 11219 0 0 19200 0 38021 0 0 64546 15067 0 0 41751 0 0 0 76306 0 278913 0.011 A 2 0 288 250 0 9 775 517 0 2961 473 0 2162 0 1 2 0 0 0 7440 0.013 0 0 309 205 0 0 892 509 0 3529 357 0 3224 0 0 0 0 0 0 9025 0.012 0 0 17372 12308 0 0 43999 33995 0 122085 26570 0 113525 0 0 0 0 0 0 369854 0.011 P 441 0 0 0 0 174 1350 1 253 521 539 0 0 0 0 1879 0 0 0 5158 0.011 502 0 0 0 0 198 2086 0 261 650 666 0 0 0 0 3309 0 0 0 7672 0.012 40224 0 0 0 0 10781 97490 0 14115 35689 41654 0 0 0 0 117791 0 0 0 357744 0.012 Y 0 0 86 0 55 0 103 0 369 0 0 0 2 0 506 4 132 0 0 1257 0.006 0 0 62 0 81 0 105 0 490 0 0 0 0 0 1125 0 198 0 0 2061 0.007 0 0 4627 0 5331 0 6833 0 24730 0 0 0 0 0 51258 0 9737 0 0 102516 0.008 V 0 0 95 93 0 4 2 194 0 6 1193 1 0 1383 1 791 169 2436 0 6368 0.014 0 0 95 98 0 0 0 191 0 0 932 0 0 2319 0 989 286 3057 0 7967 0.013 0 0 5746 6574 0 0 0 16368 0 0 49590 0 0 71113 0 59831 16149 79863 0 305234 0.011 M 55 76 0 0 3 0 2 0 1 867 0 0 0 1024 0 293 0 576 0 2897 0.017 104 107 0 0 0 0 0 0 0 705 0 0 0 1050 0 335 0 826 0 3127 0.014 7773 7449 0 0 0 0 0 0 0 38736 0 0 0 50830 0 20050 0 40683 0 165521 0.016 C 527 0 0 0 0 0 282 131 0 0 2 0 370 0 1 5 120 1 89 1528 0.008 350 0 0 0 0 0 260 116 0 0 0 0 594 0 0 0 169 0 82 1571 0.006 20075 0 0 0 0 0 14644 8198 0 0 0 0 27023 0 0 0 9466 0 5973 85379 0.008 L 244 0 0 1 0 115 303 0 112 4 3 977 1 932 258 0 878 237 58 4123 0.005 227 0 0 0 0 145 279 0 83 0 0 692 0 1078 304 0 1366 387 95 4656 0.004 20625 0 0 0 0 8890 13829 0 6199 0 0 49877 0 63501 14570 0 66499 15386 4563 263939 0.006 F 0 0 2 0 8 0 324 0 0 0 0 0 128 114 0 128 728 126 0 1558 0.005 0 0 0 0 0 0 291 0 0 0 0 0 124 159 0 144 880 117 0 1715 0.004 0 0 0 0 0 0 17184 0 0 0 0 0 6637 10060 0 9861 50019 6564 0 100325 0.006 I 25 36 0 0 107 0 100 0 1 987 0 1 0 1994 451 0 244 96 0 4042 0.012 35 30 0 0 180 0 131 0 0 1468 0 0 0 2189 690 0 337 242 0 5302 0.011 1982 1975 0 0 10201 0 7606 0 0 59179 0 0 0 91395 32522 0 18329 14037 0 237226 0.012 W 438 0 0 0 0 0 51 35 0 0 0 0 2 0 0 76 44 0 0 646 0.007 225 0 0 0 0 0 38 51 0 0 0 0 0 0 0 169 57 0 0 540 0.004 12369 0 0 0 0 0 3404 3412 0 0 0 0 0 0 0 10097 2928 0 0 32210 0.006 Patients 6724 3022 2744 2877 3032 3804 7007 3491 3935 6511 4790 3208 1458 7018 3421 2608 5271 1817 4830 1299 78867 1kg 7143 4654 2947 3326 4602 6436 9003 3695 6378 7706 4232 2380 2382 8950 5743 5728 8140 3077 6789 3000 106311 gnomAD 392825 208233 157595 176916 203630 220159 406946 231337 212851 331483 233068 172389 113960 400015 168205 207719 363996 158521 249193 94906 4703947 The data in table 1 depicting the CKD patients on the top in the row of each cell, 1kG in the middle and genomAD in the bottom. Amino acids are arranged according to one single letter nomenclature following the scale of Fauchère and Pliska according to their increasing hydrophobicity from left to right and the top to the bottom. The less hydrophobic are on the left and the most on the right. The yellow blocks indicate absence of a statistically significant difference between the CKD patients and the two data sets, the light blue cells mean there is a statistically significant difference between the CKD patients data set and 1kG, genomAD or 1 kG and genomAD together. In the column representing the total number of mutations, the green color denotes absence of mutation between the CKD patients and the two data sets while the light brown color indicates presence of significant difference between the CKD patients and the two data sets. Additional Declarations No competing interests reported. Supplementary Files supplementaryfigure1withtitle.jpg supplementaryfigure2withtitle.jpg supplementaryfigure3withtitle.jpg supplementaryfigure4withtitle.jpg Cite Share Download PDF Status: Posted Version 1 posted You are reading this latest preprint version Research Square lets you share your work early, gain feedback from the community, and start making changes to your manuscript prior to peer review in a journal. As a division of Research Square Company, we’re committed to making research communication faster, fairer, and more useful. We do this by developing innovative software and high quality services for the global research community. Our growing team is made up of researchers and industry professionals working together to solve the most critical problems facing scientific publishing. Also discoverable on Platform About Our Team In Review Editorial Policies Advisory Board Help Center Resources Author Services Accessibility API Access RSS feed Manage Cookie Preferences © Research Square 2026 | ISSN 2693-5015 (online) Privacy Policy Terms of Service Do Not Sell My Personal Information {"props":{"pageProps":{"initialData":{"identity":"rs-4268762","acceptedTermsAndConditions":true,"allowDirectSubmit":true,"archivedVersions":[],"articleType":"Research Article","associatedPublications":[],"authors":[{"id":296407651,"identity":"74388b2f-0a8d-46a3-9663-63656bec6258","order_by":0,"name":"Edem Nuglozeh","email":"data:image/png;base64,iVBORw0KGgoAAAANSUhEUgAAAZAAAAAyAQMAAABI0h/eAAAABlBMVEX///8AAABVwtN+AAAACXBIWXMAAA7EAAAOxAGVKw4bAAAA3UlEQVRIiWNgGAWjYBACgwMMjAeAdAI/iJdQQIQWC6B6sBbJBhBpQIQWG5gWgwNgS4nRciP9woEPf2zyjM+vTvzwwIBBnl/sAH4tZjdyCg7O4EkrNrvxdrME0GGGM2cnENSScJhH4nDithtnN4C0JBjcJqDFGKzF4H/i5hlnN/8gSovhjfQDh3kSDiRu4O/dRpwthmfeMByccSA5ccYN3m0WCQYShP1icDz94YMPf+wS+/vPbr75o8JGnl+agBYGBh5oXEiAVUoQUg4C7A8gNP8BYlSPglEwCkbBSAQAbQ9RphkQxC0AAAAASUVORK5CYII=","orcid":"","institution":"University of Ha’il, Saudi Arabia and College of Medicine, Ondokuz Mayıs University","correspondingAuthor":true,"prefix":"","firstName":"Edem","middleName":"","lastName":"Nuglozeh","suffix":""},{"id":296407652,"identity":"235471ac-aa1b-45f6-a90c-e327acc35420","order_by":1,"name":"Mohammad Feroze Fazaludeen","email":"","orcid":"","institution":"University of Eastern Finland","correspondingAuthor":false,"prefix":"","firstName":"Mohammad","middleName":"Feroze","lastName":"Fazaludeen","suffix":""},{"id":296407653,"identity":"3c556cf2-1bd9-4638-a997-5004cca7740a","order_by":2,"name":"Fatih Sağlam","email":"","orcid":"","institution":"Ondokuz Mayıs University","correspondingAuthor":false,"prefix":"","firstName":"Fatih","middleName":"","lastName":"Sağlam","suffix":""}],"badges":[],"createdAt":"2024-04-15 09:42:04","currentVersionCode":1,"declarations":"","doi":"10.21203/rs.3.rs-4268762/v1","doiUrl":"https://doi.org/10.21203/rs.3.rs-4268762/v1","draftVersion":[],"editorialEvents":[],"editorialNote":"","failedWorkflow":false,"files":[{"id":55631529,"identity":"4740a7a9-2d8d-4be8-9aa3-5ecf70adbf57","added_by":"auto","created_at":"2024-04-30 19:43:58","extension":"jpg","order_by":1,"title":"Figure 1","display":"","copyAsset":false,"role":"figure","size":165073,"visible":true,"origin":"","legend":"\u003cp\u003eAverage distribution of capture sub regions from exome sequencing. The distribution of mutation sites within genomic regions from different variants in CKD patients are shown as a proportion of average coverage. Nine types of regions are presented. This figure presents that, the majority of those variants are: intron variants followed by downstream and upstream extra-exonic variants, continuing to exonic sequence and intergenic variants and lastly, the splicing acceptor region represents the least region contributing to this variant’s population. This statistical reparation of the variants may represent a transition bias observed in introns, pseudogenes, and other noncoding regions (Gojobori et al. 1982;) suggesting that causes like mutations act across the entire genome.\u003c/p\u003e","description":"","filename":"Figure1withtitle.jpg","url":"https://assets-eu.researchsquare.com/files/rs-4268762/v1/8fcf47daee48a18609f1201d.jpg"},{"id":55631533,"identity":"25931804-4c3f-4b18-a4a1-34421b0b753a","added_by":"auto","created_at":"2024-04-30 19:43:58","extension":"jpg","order_by":2,"title":"Figure 2","display":"","copyAsset":false,"role":"figure","size":1748069,"visible":true,"origin":"","legend":"\u003cp\u003eHeatMap of codon changes in the CKD patients. The HeatMap shows codons exchanges frequencies in the transcripts and these exchanges reflect the cumulative distribution of codons mutability for silent (blue area), missense (yellow spots) nonsense (red spots) and this distribution of mutability itself depends on the absence or presence CpG dinucleotides islands. The inset colors show the probability density distribution by the type of mutation. The variation in colors on upper right side reflect the degree of exchanges, blue color signifies low exchanges whereas red color is associated with high exchanges. This HeatMap preludes the observations in the amino acid’s changes observed at the translational level. The codons change from Y axis to X axis.\u003c/p\u003e","description":"","filename":"Figure2withtitle.jpg","url":"https://assets-eu.researchsquare.com/files/rs-4268762/v1/67ece8efb7bf33a0529765ac.jpg"},{"id":55631532,"identity":"e460820a-853d-4e39-b085-7ed55198a782","added_by":"auto","created_at":"2024-04-30 19:43:58","extension":"jpg","order_by":3,"title":"Figure 3","display":"","copyAsset":false,"role":"figure","size":447911,"visible":true,"origin":"","legend":"\u003cp\u003eScatter plots representation comparing the mutability values in the three datasets. From left to right: (a) amino acids mutability values between CKD patients and 1000 genomes dataset, (b) amino acids mutability values between CKD patients and genomAD dataset and (c) amino acids mutability values between genomAD and 1000 genome databases. There is a strong correlation in terms of mutability between all the datasets.\u003c/p\u003e","description":"","filename":"Figure3withtitle.jpg","url":"https://assets-eu.researchsquare.com/files/rs-4268762/v1/b381e95c75c275ea886d78ea.jpg"},{"id":55631531,"identity":"93a1b64b-2d4d-4ecb-b879-fe82fca6a0ef","added_by":"auto","created_at":"2024-04-30 19:43:58","extension":"jpg","order_by":4,"title":"Figure 4","display":"","copyAsset":false,"role":"figure","size":1520421,"visible":true,"origin":"","legend":"\u003cp\u003eBio-bar representations showing the comparison of the observed differences in the % of mutations from a single amino acid mutating to all other amino acids proportionally in the three datasets: the 1 kg (red), genomAD (green) and CKD patients (blue) datasets. For e.g., in CKD dataset, more mutations are recorded for: Tryptophan, Histidine, Glycine and Lysine and finality of the mutation of these four amino acids converge all to Arginine (p\u0026lt;0.0001) in term of mutability and Methionine and Isoleucine both mostly change into valine (p\u0026lt;0.0001).\u003c/p\u003e","description":"","filename":"Figure4.jpg","url":"https://assets-eu.researchsquare.com/files/rs-4268762/v1/c41dd1c52c8c0ae996064e80.jpg"},{"id":55631530,"identity":"e3de528c-ab85-4c19-9220-ec720c0a76b0","added_by":"auto","created_at":"2024-04-30 19:43:58","extension":"jpg","order_by":5,"title":"Figure 5","display":"","copyAsset":false,"role":"figure","size":883097,"visible":true,"origin":"","legend":"\u003cp\u003eAmino acid mutability hierarchy plot comparing the mutability scores for 1 kG, genomAD and CKD patients. The most mutable amino acids are at the top and the least mutable in the bottom. Correlation coefficient between CKD vs 1 kg, CKD vs genomAD are respectively: 0.9353 and 0.8947\u003c/p\u003e","description":"","filename":"Figure5withtitle.jpg","url":"https://assets-eu.researchsquare.com/files/rs-4268762/v1/c0add4804357e977993bc277.jpg"},{"id":55631534,"identity":"76d14087-8e3c-4c26-b0d5-10bccaab3295","added_by":"auto","created_at":"2024-04-30 19:43:59","extension":"jpg","order_by":6,"title":"Figure 6","display":"","copyAsset":false,"role":"figure","size":462098,"visible":true,"origin":"","legend":"\u003cp\u003eThe distribution of average protein mutabilities for all human proteins in the 1 kG, genomAD and CKD patients. The average proteins mutability shows that all amino acids proportionally show higher mutability in genomAD dataset compared to 1 kg and CKD dataset and the average proteins mutability in CKD as well as in 1 kg are equally comparable.\u003c/p\u003e","description":"","filename":"Figure6withtitle.jpg","url":"https://assets-eu.researchsquare.com/files/rs-4268762/v1/b9829e61f322eda69e4e2c8a.jpg"},{"id":84498292,"identity":"c3355bb6-92a6-4bb9-b0a1-8bf6354c7065","added_by":"auto","created_at":"2025-06-12 16:01:39","extension":"pdf","order_by":0,"title":"","display":"","copyAsset":false,"role":"manuscript-pdf","size":7250160,"visible":true,"origin":"","legend":"","description":"","filename":"manuscript.pdf","url":"https://assets-eu.researchsquare.com/files/rs-4268762/v1/76224f27-9d59-4b4a-8a62-093d1b525fd8.pdf"},{"id":55631538,"identity":"89407d48-fede-463f-82b1-97e11a2b2106","added_by":"auto","created_at":"2024-04-30 19:43:59","extension":"jpg","order_by":8,"title":"","display":"","copyAsset":false,"role":"supplement","size":738291,"visible":true,"origin":"","legend":"","description":"","filename":"supplementaryfigure1withtitle.jpg","url":"https://assets-eu.researchsquare.com/files/rs-4268762/v1/8a34361a58cb5c23cbae4792.jpg"},{"id":55632331,"identity":"0366bcc5-670a-4a07-93d3-bbc50b7492cc","added_by":"auto","created_at":"2024-04-30 19:51:59","extension":"jpg","order_by":9,"title":"","display":"","copyAsset":false,"role":"supplement","size":664087,"visible":true,"origin":"","legend":"","description":"","filename":"supplementaryfigure2withtitle.jpg","url":"https://assets-eu.researchsquare.com/files/rs-4268762/v1/2c0cf63a029e549df77b711d.jpg"},{"id":55631535,"identity":"bf64fb19-7f7a-4349-8f0e-19ac471dabe4","added_by":"auto","created_at":"2024-04-30 19:43:59","extension":"jpg","order_by":10,"title":"","display":"","copyAsset":false,"role":"supplement","size":735780,"visible":true,"origin":"","legend":"","description":"","filename":"supplementaryfigure3withtitle.jpg","url":"https://assets-eu.researchsquare.com/files/rs-4268762/v1/cddfcfca52e76561d0fa4996.jpg"},{"id":55631536,"identity":"50f3ef4b-0b71-4286-b1ac-1082574ee068","added_by":"auto","created_at":"2024-04-30 19:43:59","extension":"jpg","order_by":11,"title":"","display":"","copyAsset":false,"role":"supplement","size":694106,"visible":true,"origin":"","legend":"","description":"","filename":"supplementaryfigure4withtitle.jpg","url":"https://assets-eu.researchsquare.com/files/rs-4268762/v1/8a0d707a1414ef27f9a740b4.jpg"}],"financialInterests":"No competing interests reported.","formattedTitle":"Amino acids exchange obtained from CKD patients via Exome Sequencing differ radically from those of natural variants 1000 genome and genomAD databases","fulltext":[{"header":"1. Background","content":"\u003cp\u003eDNA is an adaptable and dynamic molecule. As such, the nucleotides residing inside the DNA molecule undergo through multiple permutations under an evolutional process called mutation and this process spans the entire human genome. Some of these mutations can be harmless, beneficial or deleterious to human being according to the nature of the mutation. We are invariably trained under the paradigm that all biological activities in cells are embedded in three letters code that fall under the denomination as genetic codes. The change in genetic code has long been seen as the main vectors of genetic diseases and these diseases ignite as the hurtful mutations or deleterious mutations that take over the biological system. These mutations have direct impact on amino acids sequences and it was shown that the disease-causing variants usually provoke drastic changes of amino acid physico-chemical properties of proteins such as charge, hydrophobicity and geometry arrangement [1]. Variants involved in diseases tend to cause more changes of hydrogen bond network and salt bridges as compared with harmless amino acid mutations [2,3]. Diseases-associated variants target the more conserved sequences in genome that relatively remained unchanged far back in the phylogenic tree as observed in 1 kG database [4]. However, most of phenotypical effects and molecular cause of origin of most variants remain elusive so anticipating or predicting a single amino acid change in a specific disease will be of great medical interest. Genetic variants underlying common disease may vary in frequency across population more than random variants do in the genome, perhaps because of their exposition to epigenetics events due to natural selection [5]. The Next-generation sequencing (NGS) is instrumental in the discovery of growing number of novel candidate\u0026rsquo;s genes variants and most importantly rare variants in pharmacogenes [6].\u0026nbsp;\u003c/p\u003e\n\u003cp\u003eThe 1000 Genomes Project was developed to serve as a big repertoire and global reference for human genetic variation and is used to serve as a baseline for subsequent research in establishing the relationship between genotype and phenotype and ultimately identifying the genetic basis of human disease [7]. Basically, the 1 kG database serves as a reference where researchers can vet multiple SNPs resulting from exome and genome sequencing.\u003c/p\u003e\n\u003cp\u003eBesides the 1kG database, the genome aggregation database or genomAD was also developed with the goal of accumulating and harmonizing both exome and genome sequencing data from a wide variety of large-scale sequencing projects. The most recent data set (gnomAD v2.1) provides access to more than 125,000 exome and 15,000 whole-genome sequences from unrelated and healthy adults sequenced as part of various disease-specific and population genetic studies. It has accumulated 15708 whole genome and 125748 of exomes. Its predecessor, the Exome Aggregation Consortium (ExAC) has been mentioned in more than 4,000 publications [8]. The genomAD includes the genomes and exomes from European, Latino African, African American, South East Asian, Ashkenazi Jewish and other population. The gnomAD papers reported 241 million small genetic variants (single nucleotide variants and short insertion/deletion variants) and 335,470 structural variants (DNA rearrangements of at least 50 base pairs), compared with 7.4 million small genetic variants identified in (ExAC). Recently, the gnomAD team is already expanding the resource further and has recently released gnomAD v3, which contains 71,702 genomes.\u0026nbsp;\u003c/p\u003e\n\u003cp\u003eThe Genome Aggregation Database (gnomAD) has paved the road to reveal the spectrum of mutational constraints affecting human protein-coding genes in a catalog predicting loss-of-function variants in 125,748 whole-exome and 15,708 whole-genome sequencing datasets\u0026nbsp;[8], analysis and prediction loss-of-function variants from 125,748 human exomes and 15,708 whole genomes. It also provides a roadmap for human \u0026lsquo;knockout\u0026rsquo; studies into disease biology and drug-target selection [4] and large empirical assessment that provides a reference map for disease-association studies, population genetics, and diagnostic screening [9].\u003c/p\u003e\n\u003cp\u003eOne way of discovering the function of a gene is to study what happens when the gene is disrupted by a mutation. These variants often have adverse outcomes and are usually rare. Large genetic sequencing studies provide an opportunity to examine the effects of these loss-of-function variants, which could provide important insights into human biology and diseases [10].\u0026nbsp;\u003c/p\u003e\n\u003cp\u003eWith the existence of myriad of variants datasets, the establishment of novel disease-datasets becomes promising. It was in this optic that we began the study of chronic kidney failure disease (CKD) with hope to establish a nsSNPs for this disease.\u003c/p\u003e\n\u003cp\u003eChronic kidney disease (CKD) is a major global health problem and affects approximately one in ten adults worldwide [11]. Both genomic and environmental factors contribute to this complex heterogeneous disease. CKD heritability is estimated to be high (30\u0026ndash;75%). Although the estimation of Mendelian disorders is supposed to be responsible for 10% of ESRD cases [12], 15%\u0026ndash;30% of patients, including those with presumably acquired forms of disease such as diabetic or hypertensive nephropathy, report a family history of renal disease. This indicates the existence of a contribution of hereditary factors across clinical categories [13].\u0026nbsp;\u003c/p\u003e\n\u003cp\u003eMoreover, affected individuals within the same family frequently carry different clinical diagnoses or spectrum, suggesting that they may be sharing genetic contributions across CKD subtypes [13] and recent studies support this hypothesis [14]. For example, two variants in \u003cem\u003eAPOL1\u003c/em\u003e (Online Mendelian Inheritance in Man reference number [OMIM]: 603743) significantly increase the risk for multiple forms of CKD, including focal segmental glomerulosclerosis (FSGS), hypertension-attributed nephropathy, and HIV-1\u0026ndash;associated nephropathy [15]. \u0026nbsp;In similar way, mutations in the type-4 collagen genes (\u003cem\u003eCOL4A3\u003c/em\u003e [OMIM: 120070], \u003cem\u003eCOL4A4\u003c/em\u003e [OMIM: 120131], and \u003cem\u003eCOL4A5\u003c/em\u003e [OMIM: 303630]) traditionally associated with Alport syndrome can also manifest frequently as FSGS [16].\u0026nbsp;\u003c/p\u003e\n\u003cp\u003eCollectively, these findings highlight the potential of an in depth of genetic and sequencing studies to identify the shared causative variants spanning all the spectrum of CKD and ultimately undertake clinical studies to uproot the basis of underlying molecular pathophysiological causes of CDK.\u0026nbsp;\u003c/p\u003e\n\u003cp\u003eTo address some part of this issue, we conducted exome sequencing on gDNA of 12 young patients suffering of kidney failure. After bioinformatics analysis of our exome sequencing data, more than 250 SNPs per sample were retained as variants of interest. Combined harder filtrations are operated on these presumptive SNPs which narrowed them down to two single SNPs (data not shown) as these results will be reported separately in another publication aimed at addressing the functionality of those genes. Recently, we also reported and published karyotyping and chromosome HeatMap of some regional genomic of interest from the same CKD patients [17].\u003c/p\u003e\n\u003cp\u003eHere we sought to establish and describe the relationship between PAM matrices obtained from these CDK patients that we separately established and compared them to 1000 genome and genomAD dataset matrices thus allowing us to derive and compare the combined mutability of each amino acids derived from CDK patients as well as the amino acids from the two datasets, 1kG and genomAD. These measures allow us to establish the ranking mutabilities of the amino acids among the three data sets as well as a profile of amino acids mutations that can be damageable in disease situation like CKD.\u003c/p\u003e"},{"header":"2. Methods","content":"\u003cp\u003e\u003cstrong\u003e\u003cem\u003e2.1. Objective\u003c/em\u003e\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eThis study has four specific objectives:\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e1\u003c/strong\u003e. To sequence the human genome from patients suffering from chronic kidney disease, on\u003c/p\u003e\n\u003cp\u003eIllumina-MiSeq platform.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e2\u003c/strong\u003e. Exploring the possibilities of correlation between plasma and urinary kidney profile and some biochemical parameters, as well of association between \u003cstrong\u003eknown phenotypic SNPs and amino acids exchange.\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e3\u003c/strong\u003e. Investigating the existence of deleterious amino acids exchange.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e4\u003c/strong\u003e. Authenticating these exchanges on phenotypic basis by reconstructing the variant genes harboring these mutations paving the way for future development of animal models for ex\u003cem\u003e vivo\u003c/em\u003e\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e\u003cem\u003e2.2. Genomic DNA library preparation and sequencing\u003c/em\u003e\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eHigh quality gDNA was purified from lymphocytes whole as described elsewhere. The construction of the library was conducted using the Nextera Rapid Capture kits (Illumina)\u003c/p\u003e\n\u003cp\u003e50 ng of gDNA was utilized using transposase-based chemistry to create exome libraries\u003c/p\u003e\n\u003cp\u003eLibrary was Qc on Bioanalyzer 2100, (Agilent Technology, Santa Clara, CA) to assess the integrity and size library fragments\u003c/p\u003e\n\u003cp\u003e2 x 75 paired end cycles were performed (+1 cycle to each forward and reverse read to allow for phasing/pre-phasing).\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e\u003cem\u003e2.3. Bioinformatics analyses\u003c/em\u003e\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eThe flow chart for bioinformatics analysis have been published by our team elsewhere.\u003c/p\u003e\n\u003cp\u003eBelow are summarized successive steps we used in bioinformatics analysis.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e\u003cem\u003ea. Read Trimming and Clipping of Adapters\u003c/em\u003e\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eReads are trimmed from the 3' end to have at least a phred score of \u003cstrong\u003e30\u003c/strong\u003e. Illumina sequencing adapters are removed from the reads, and all reads are required to have a length of at least \u003cstrong\u003e50\u003c/strong\u003e bp. Trimming and clipping are performed using Trimmomatic(Bolger, Lohse, and Usadel 2014) [18]. This step generated: Samples Readset, Raw pair Read, number of Paired Reads obtained from the sequencer, the number of Remaining Paired Reads after the trimming step and the percentage of Surviving Paired Reads and Raw Paired Reads.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e\u003cem\u003eb. Read Alignment to a Reference Genome\u003c/em\u003e\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eThe filtered reads are aligned to a reference genome. The genome used in this analysis is \u003cem\u003e\u003cstrong\u003eHomo_sapiens\u003c/strong\u003e\u003c/em\u003e assembly \u003cstrong\u003ehg19\u003c/strong\u003e. Each readset is aligned using \u003cstrong\u003eBAW\u003c/strong\u003e [Li and Durbin (2010)] [19] which creates a Binary Alignment Map file (bam). Then we merged all readset \u003cstrong\u003eBAM\u003c/strong\u003e files from the same sample into a single global \u003cstrong\u003eBAM\u003c/strong\u003e file using \u003cstrong\u003ePicard\u003c/strong\u003e.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eBWA\u003c/strong\u003e is a fast light-weighted tool which aligns relatively short sequences (queries) to a sequence database (target), such as the human reference genome. It is based on the Burrows-Wheeler Transform\u003cstrong\u003e (BWT). BWA\u003c/strong\u003e is designed for short queries up to ~200 bp with low error rate (\u0026lt; 3%). It does gap global alignment, supports paired-end reads, and is one of the fastest short read alignment algorithms to date while also visiting suboptimal hits.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e\u003cem\u003ec. Read Alignment Improvement\u003c/em\u003e\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eBecause of lack of perfect aligner tool, the alignment step remains really sensitive to the aligner parameters as well as technical and biological variations. To increase the quality and speed of subsequent variant calling, we performed a series of procedures to improve the alignment. These procedures consist of realigning the surrounding short insertions or deletions, fixing possible read mate discrepancy due to realignment marking duplicated reads and recalibrating read base quality.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e\u003cem\u003ed. Realigning Short Insertions and Deletions (INDELs)\u003c/em\u003e\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eThe realignment is done using \u003cstrong\u003eGATK\u003c/strong\u003e (DePristo et al. 2011) [20]. INDELs in reads (especially near the ends) can trick the mappers into mis-aligning with mismatches. These artifacts resulting from mismatches can harm base quality recalibration and variant detection. Realignment around INDELs helps to improve the accuracy of several downstream steps.\u003c/p\u003e\n\u003cp\u003eInsertion and deletion realignment is performed on regions where multiple base mismatches are preferred over INDELs by the aligner since it appears to be less costly for the algorithm. Such regions will introduce false positive variant calls which may be filtered out by realigning those regions properly. Mainly realignment will occur in 3 different region types: (1) Known sites (e.g., dbSNP, 1000 Genomes), (2) INDELs seen in original alignments (in CIGARs) (3) Sites where evidence suggests a hidden INDEL.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e\u003cem\u003ee. Fixing Read Mates\u003c/em\u003e\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eOnce local regions are realigned, the read mate coordinates of the aligned reads need to be recalculated since the reads are realigned at positions that differ from their original alignment. The read mate positions fixing is performed using multi-task application Picard and will be subsequently used to mark duplicates\u003cstrong\u003e.\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e\u003cem\u003ef. Marking Duplicates\u003c/em\u003e\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eBecause Exome Sequencing experiment encompasses several PCR amplifications steps which could induce coverage bias during the library construction, this bias could generate high level of false positives and false negatives during the variant calling steps (SNV, SV and CNV). Thus, removing or marking read duplicates using Picard is an important step of the sequencing analysis. Aligned reads are duplicates if they have the same 5' alignment positions (for both mates in the case of paired-end reads). All but the best pair (based on alignment score) will be marked as a duplicate in the bam file. Duplicates reads will be excluded in the subsequent analysis.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e\u003cem\u003eg. Base Quality Recalibration\u003c/em\u003e\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eThis step allows recalibrating base quality scores of sequencing-by-syntheses reads in an aligned BAM file. After recalibration, the quality scores in the QUAL field in each read in the BAM output are more accurate in that, the reported quality score is closer to its actual probability of mismatching to the reference genome. QUAL represents the accuracy of the genotyping and when QUAL is 20, this means that there is 99% probability that there is a variant at the site. The recalibration process is accomplished by analyzing the covariation among several features of a base. For example: (1) Reported quality score, (2) the position within the read and (3) the preceding and current nucleotide (sequencing chemistry effect) observed by the sequencing machine. These covariates are then subsequently applied through a piecewise tabular correction to recalibrate the quality scores of all reads in a BAM file. The recalibration process is performed using \u003cstrong\u003eGATK \u003c/strong\u003e(DePristo et al. 2011) [20]\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e\u003cem\u003eh. Sequencing and Alignment Metrics per Sample\u003c/em\u003e\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eThe aim of this step is to provide each sample a general summary statistics and Sample readsets are merged for clarity.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e\u003cem\u003ei. SNV Annotations\u003c/em\u003e\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eAn in-house database identifies regions in which reads are confidently mapped to the reference genome. Generally, low mappability corresponds to RepeatMasker regions and decreases substantially with the increasing in the read length. A region is identified as \u003cstrong\u003eHC\u003c/strong\u003e = coverage too high, \u003cstrong\u003eLC\u003c/strong\u003e = low coverage, \u003cstrong\u003eMQ\u003c/strong\u003e = too low mean mapQ (\u0026lt; 20) and \u003cstrong\u003eND\u003c/strong\u003e = unmappable region (no data) at the position.\u003c/p\u003e\n\u003cp\u003eThe VCF files are also annotated for:\u003c/p\u003e\n\u003col\u003e\n\u003cli\u003edbSNP using the SnpSift software (Cingolani, Patel, et al. 2012) [21].\u003c/li\u003e\n\u003cli\u003eVariant effects (predicted variant effects on gene, such as amino acid changes) using the SnpEff software (Cingolani, Platts, et al. 2012) [21].\u003c/li\u003e\n\u003c/ol\u003e\n\u003cp\u003eThe SnpSift http://snpeff.sourceforge.net/SnpSift.html software which is a toolbox used to filter and localize missense which are number of variants in coding region for which the variation generates a codon modification. This lead to generate two types of variant metrics tables: variants for codons changes and amino acids changes induced by SNV.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e\u003cem\u003ej. Variants Metrics\u003c/em\u003e\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eThe variant metrics and statistics have been generated using the SnpEff software (Cingolani, Platts, et al. 2012) [21].\u003c/p\u003e\n\u003cp\u003eThe variant metrics and statistics have been generated using the SnpEff software (Cingolani, Platts, et al. 2012) [21].\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e2.4. Non-synonymous mutations in humans\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eWe query two reference data sets for natural human variants that we used work. The first set of natural variants was from the 1000 Genomes Project (1kG), and the second from gnomAD. The 1kG data comprises a compilation of human DNA variants from 1092 individuals from diverse populations across the world. Only variants with a frequency of occurrence of \u0026gt;1% were included. To avoid the presence of unstable elements, major histocompatibility and immunoglobulin were removed from group of the transcripts. Of interest here were the variants that mapped to protein coding regions as synonymous (sSNPs) and non-synonymous (nsSNPs) variants. These were obtained from Ensembl [22] v67, as described in de Beer et al [1].\u003c/p\u003e\n\u003cp\u003eThe other source of natural variants was gnomAD, which contains data from various disease-specific and population genetic studies. We used v.2.0 which had variants from over 140,000 individuals. The data were downloaded from the Broad Institute\u0026rsquo;s web site. As with the 1kG data, the genome coordinates had to be converted to the corresponding sSNPs and nsSNPs in the relevant protein coding regions to get the amino acid changes involved.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e2.5. Non-synonymous mutations in humans from CKD Patients\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eAs initially reported in section bioinformatics analysis, each transcript representative for each protein sequence obtained from the VCF files was allocated Ensembl ID using the mapping tool provided by Uniprot. We derived nsSNPs for each protein from CKD from VCF files using SnpEff software and the metrics converted into two tables with one representing codon change and the other one amino acids exchange with each record of entry on Y-axis symbolized by one single letter amino acid. Because, major histocompatibility complex and immunoglobulins are inherently unstable, they were removed from the pool of the transcripts The data set representative of amino acids exchanges is later converted into amino acid pair score matrices or exchange frequencies among amino acids.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e2.6. Statistical Analysis\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eWe calculated the Pearson correlation coefficient (r\u003csub\u003eP\u003c/sub\u003e) to examine the linear relationship between the variables and the Spearman correlation coefficient (r\u003csub\u003eS\u003c/sub\u003e) to examine the monotonous relationship over sequence numbers. We interpreted the obtained correlations data as strong relationship if 0.7 \u0026lt; |r| \u0026le; 1, as moderate relationship when 0.4 \u0026lt; |r| \u0026le; 0.7, and for weak or absence of relationship if 0 \u0026le; |r| \u0026le; 0.4. We analyzed the differences in the mutation numbers between the Patients, 1kg on one hand the patients and gnomAD datasets using Fisher's exact test. We applied Bonferroni correction to the p-values when examining multiple comparisons. We obtained all analysis results and graphics using the R package program (R Core Team, 2021) [23].\u003c/p\u003e\n\u003cp\u003eWe will have weak correlation, if 0 \u0026le; |r| \u0026le; 0.4, moderate correlation, if 0.4 \u0026lt; |r| \u0026le; 0.7 and strong correlation if 0.7 \u0026lt; |r| \u0026le; 1\u003c/p\u003e"},{"header":"3. Results","content":"\u003cp\u003eThis project was carried out to compare the amino acids exchange from CKD patients databases compared to the amino acids exchanges from 1000 genome and genomAD databases. The data from CKD patients were obtained by carrying out exome sequencing on genomic DNA libraries built from the patients genomic DNA (see methods). We already published the biochemical profiles from these patients in Eur. J. Med. Health. Sci [17}. The Average distribution of capture sub regions from exome sequencing is presented on Fig 1. This distribution of mutation sites within genomic regions from different variants in CKD patients is distributed to nine genomic regions. This statistical repartition of the variants may represent a transition bias observed in introns, pseudogenes, and other noncoding regions (Gojobori et al. 1983;) [24] The biochemical pipelines and ANOVAR tool we used for the bioinformatic analysis of the FASTQ data are presented were published elsewhere [17]. These were instrumental in experimental determination nsSNPs which were filtered and annotated with respect to their functions. In Fig 2, we presented the codons HeatMap changes in CKD patients. The codons exchange frequencies in the transcripts reflect the cumulative distribution of codons mutability for silent (blue area), missense (yellow spots) nonsense (red spots) and this distribution of mutability itself depends on the absence or presence CpG dinucleotides islands. The inset colors show the probability density distribution by the type of mutation. The variation in colors reflect the degree of exchanges: blue color signifies low exchanges whereas red color is associated with high exchanges. In table 1, we presented the amino acids exchanges in CKD patients, together with the amino acids\u0026rsquo; exchanges derived from the 1000 genome and genomAD databases.\u0026nbsp;\u003c/p\u003e\n\u003cp\u003eWe carried out the exome sequencing project in patients with CKD in part to retrieve all nsSNPs and their associated transcripts. These SNPs were submitted to successive bioinformatic analysis and underwent through many steps of hard filtering (see method) to ascertain that, just all pathological SNPs of interest were retained from which we produced a square matrice 20x20 of amino acids substitution from CKD patients. We also simultaneous carried out analysis of amino acids exchange matrix generated from 1091 individuals obtained from 1000 genome dataset and 140,000 individuals from genomAD database. The CKD matrix combined with the 1 kg matrix and the genomAD matrix presented in table 1 depicted an asymmetric configuration in term of topology which itself is inherent to the difference in mutability of different codons and the pathological state of different proteins in CKD samples [25, 26]. This difference in mutability is due in part by flanking nucleotides context of the mutation site. Indeed, it has been reported that up one heptamers, 3 nucleotides upstream and 3 nucleotides downstream of the site of nsSNPs, can affect the mutation [27-30]. For example, the elevation in mutation rate is due to methyl cytosine deamination at CpG dinucleotides [31] and more specifically, mutability stemming from nonsynonymous mutations depends on the specificality of the amino acids that are exchanged, reflecting differences in both physicochemical properties [32] and metabolic effects [33].\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e3.1. Mutability of amino acids in CKD, 1000 genome and genomAD Matrix\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eThe mutability of the amino acids in the three databases are summarized on table 1. Each cell contains information about each amino acid from the three databases, with on the top, the CKD, in the middle the 1 kg and genomAD in the bottom and the subsequent presentation of the rest of our results in this table will follow this order. Talking about the mutability of the amino acids among the three databases, Arginine remains the most mutable amino acid all tree databases with the mutability metrics organized respectively from the top to the bottom in its cell is (0.022, 0.030 and 0.021) for the three databases. Inside the cell, Arginine mutability from 1000 genome dataset remains higher \u003cem\u003evis a vis\u003c/em\u003e to Arginine mutability in CKD database which itself is higher than Arginine mutability in genomAD dataset. However, those amino acids with more chemical complexity structures like: Tryptophan and Phenylalanine respectively depict the lowest mutabilities values for the three datasets (CKD, 1 kg and genomAD) with Tryptophan mutability being (0.007, 0.004 and 0.006) respectively for the three databases and Phenylalanine mutability being (0.005, 0.004 and 0.006) respectively.\u0026nbsp;\u003c/p\u003e\n\u003cp\u003eWe also compared the probabilistic distribution of amino acids in human proteome between the three datasets (see \u003cstrong\u003efigure S1\u003c/strong\u003e). On Y axis is shown the number of mutations of amino acids and on X axis we presented the frequency of occurrence of the amino acids in human proteome. From this result, it is clear that \u003cem\u003eArginine\u003c/em\u003e and \u003cem\u003eLeucine\u003c/em\u003e represent the outliers in that they deviate from the common alignment on the axe from other amino acids. The result also shows moderate correlation between the mutability and the probabilistic distribution of the amino acids in human proteome in the three datasets with their correlation coefficients being: (\u003cstrong\u003er\u003csub\u003eCKD\u003c/sub\u003e = 0.6062, r\u003csub\u003e1kg\u003c/sub\u003e = 0.4808, r\u003csub\u003egenomAD\u003c/sub\u003e = 0.6430\u003c/strong\u003e). The same moderate positive correlation is also observed in (\u003cstrong\u003efigure S2\u003c/strong\u003e). The analysis of data from 1 kg dataset presents the relationship between mutabilities and the number of codons with the correlation coefficient being (\u003cstrong\u003er\u003csub\u003e1kg\u003c/sub\u003e = 0.4334\u003c/strong\u003e) whereas data from CKD and genomAD datasets show week correlation with the correlation coefficients representing the relation between their mutabilities and their number of codons being (\u003cstrong\u003er\u003csub\u003eCKD\u003c/sub\u003e = 0.3108, r\u003csub\u003egenomAD\u003c/sub\u003e = 0.2852\u003c/strong\u003e) respectively. Contrarily to moderate and weak correlation values observed between the number of codons and their mutabilities on one hand, on the other hand, the comparison of mutabilities between the three datasets presented on fig \u003cstrong\u003e3\u003c/strong\u003e shows strong correlation with their respective correlation coefficient comparison being: (r\u003csub\u003eCKD vs 1kg\u0026nbsp;\u003c/sub\u003e=0.9225\u003csub\u003e,\u0026nbsp;\u003c/sub\u003er\u003csub\u003eCKD vs genomAD\u0026nbsp;\u003c/sub\u003e= 0.9431 and r\u003csub\u003egenomAD vs 1kg\u003c/sub\u003e = 0.9486). This is a clear demonstration that, on the evolutionary basis, the distance between proteins from the three datasets is close since it is generally accepted that more substitutions of amnio acids are needed to change one evolutionary sequence into another one and the more substitutions we have, the larger becomes the evolutionary distance [34]. Besides, the evolutionary property also depends on some amino acid properties like isoelectric point, polarity and volume [35].\u0026nbsp;\u003c/p\u003e\n\u003cp\u003eThe close evolution distance between the three databases as observed on fig \u003cstrong\u003e3\u003c/strong\u003e is also reiterated on (figure \u003cstrong\u003eS3\u003c/strong\u003e) where we show strong correlation between the mutability and the number of mutations at least in CKD and 1 kg datasets and moderate correlation in genomAD database, with 1000 genome dataset being (r\u003csub\u003e1000 genome\u003c/sub\u003e = 0.8702), followed by CKD patients (r\u003csub\u003eCKD\u003c/sub\u003e = 0.7002) moderate correlation in genomAD dataset (r\u003csub\u003egenomAD\u003c/sub\u003e = 0.6442).\u003c/p\u003e\n\u003cp\u003eThe figure S4 compares the number of mutations to the natural occurrence of amino acids in human proteome and the three databases depicted moderate correlation between the number of mutations and the natural occurrence of amino acids. Indeed, it was reported that variability in mutation is context-depend [36-38], and it is well known that, the prediction of mutation variability rate in the human genome is linked to the environment surrounding the sites of mutation [36-38]. Voight and Aggarwala [36] reported from the variant site that, three nucleotides upstream positions and downstream positions surrounding the site of the mutation affect the mutation, which means that up to 7-mer sequence context is detrimental for the mutation to take place.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e3.2. Nature of amino acids exchange in CKD, 1000 genome and genomAD databases\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eThe profile of one single amino acid changing to all other 19 amino acids in human proteome in all three datasets is portrayed on fig \u003cstrong\u003e4\u003c/strong\u003e and this is depicted as % of change one amino acid to all other amino acids and the frequency of the occurrence of different exchanges is clearly depicted between different amino acids. \u0026nbsp;For example, in the CKD patient\u0026rsquo;s dataset, more mutations are recorded for: Tryptophan (\u003cstrong\u003eW\u003c/strong\u003e), Histidine (\u003cstrong\u003eH\u003c/strong\u003e), Glycine (\u003cstrong\u003eG\u003c/strong\u003e) and Lysine (\u003cstrong\u003eK\u003c/strong\u003e) and these four later four amino acids have Arginine as an end product in term of mutability (p\u0026lt;0.0001) and both Methionine (\u003cstrong\u003eM\u003c/strong\u003e) and Isoleucine (\u003cstrong\u003eI\u003c/strong\u003e) being mostly changed into valine (\u003cstrong\u003eV\u003c/strong\u003e) (p\u0026lt;0.0001). We should recall that (\u003cstrong\u003eM\u003c/strong\u003e and\u0026nbsp;\u003cstrong\u003eI\u003c/strong\u003e) are hydrophobic amino acids with aliphatic chain. In the concept of exchangeability, (\u003cstrong\u003eI\u003c/strong\u003e) which is hydrophobic aliphatic amino acid will preferably be substituted by another hydrophobic amino acid, particularly aliphatic amino acids and this assertion is true for\u0026nbsp;\u003cstrong\u003eM\u003c/strong\u003e too [39]. On the structural basis, being hydrophobic, (\u003cstrong\u003eI\u003c/strong\u003e) prefers to be buried in hydrophobic protein cores besides being C\u0026beta;-branched like (\u003cstrong\u003eV\u003c/strong\u003e) and Threonine (\u003cstrong\u003eT\u003c/strong\u003e). Then, in substrates recognition and hydrophobic ligands binding basis, (I) and M can easily be substituted to V [39]. \u0026nbsp;\u003c/p\u003e\n\u003cp\u003eThe amino acid substitutions in diseases have well been documented [40]. Amino acids share common properties and several classifications has been adopted and sometimes, it is difficult to put all amino acids of the same group into a one invariant group because,\u0026nbsp;each amino acid in a different protein environment will have different characteristics and one cannot \u003cem\u003ea priori\u003c/em\u003e determine its role in the protein based on hydrophobicity or polarity and no-polarity nature.\u0026nbsp;\u003c/p\u003e\n\u003cp\u003eOn large scale of naturally occurring of human amino acid variations, it was demonstrated that there is a preference for some amino acid substitutions to be associated with diseases as it is frequently observed for the Arginine [40].\u003c/p\u003e\n\u003cp\u003eThe other way of classifying amino acids is the use of mutation substitution (PAM) matrix. High value in this matrix is indicative that substitution often seen in nature is favorable and \u003cem\u003evice versa\u003c/em\u003e. Mutation matrices are used as a rough guide for how good or bad a particular change will be. Another useful aspect of this concept is that, the matrix can be calculated for different datasets, most especially in diseases situation. We have generated the mutation (PAM) matrix for CKD and came up with particular specific features in amino acids changes characterizing four amino specific acids: \u0026nbsp;Tryptophan (\u003cstrong\u003eW\u003c/strong\u003e), Histidine (\u003cstrong\u003eH\u003c/strong\u003e), Glycine (\u003cstrong\u003eG\u003c/strong\u003e) and Lysine (\u003cstrong\u003eK\u003c/strong\u003e) all together changing to Arginine (\u003cstrong\u003eR\u003c/strong\u003e) and this confirmed previous past observation with Arginine (\u003cstrong\u003eR\u003c/strong\u003e) being frequently associated with diseases states [40]. \u0026nbsp;\u003c/p\u003e\n\u003cp\u003eTryptophan (\u003cstrong\u003eW\u003c/strong\u003e) is an aromatic amino acid, but its uniqueness in term of chemistry and size means that its replacement by anything else will be disastrous and we are encountering this the situation in CKD. This drastic situation in term of exchangeability between amino acids of different groups is seen with Histidine (\u003cstrong\u003eH\u003c/strong\u003e) too which is generally considered to be a polar amino acid, however its uniqueness with regard to its chemical properties makes of (\u003cstrong\u003eH)\u003c/strong\u003e not a particularly good candidate for substitution with any other amino acid. However, (\u003cstrong\u003eH\u003c/strong\u003e) was also changed to (\u003cstrong\u003eR\u003c/strong\u003e) which is a positively-charged, polar amino acid.\u003c/p\u003e\n\u003cp\u003eArginine (\u003cstrong\u003eR\u003c/strong\u003e) generally prefers to be on the surface of the protein, but its amphipathic nature means that part of the side chain is buried.\u0026nbsp;\u003c/p\u003e\n\u003cp\u003eLysine (\u003cstrong\u003eK\u003c/strong\u003e) can be substituted by Arginine (\u003cstrong\u003eR\u003c/strong\u003e) or other polar amino acids. In the determination of the involvement of (\u003cstrong\u003eK\u003c/strong\u003e) biological activity in protein function, the substitution of (\u003cstrong\u003eK\u003c/strong\u003e) with (\u003cstrong\u003eR\u003c/strong\u003e) completely eliminates the biological activity of TGF-\u0026alpha; [41].\u0026nbsp;\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e3.3. Amino acid mutability Hierarchy Scores\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eThe mutability scores of the amino acids are depicted on fig\u0026nbsp;\u003cstrong\u003e5\u003c/strong\u003e and among the three databases, the most mutable amino acids remain again the Arginine (\u003cstrong\u003eR\u003c/strong\u003e). Arginine (\u003cstrong\u003eR\u003c/strong\u003e) besides of being encoded by six codons, it harbors two\u0026nbsp;\u003cstrong\u003eCpG\u003c/strong\u003e units and has thus has higher\u0026nbsp;the potential mutability propensity and targetability as compared to Methionine (\u003cstrong\u003eM\u003c/strong\u003e) which is coded by one single codon, but still performs well in term of mutability score.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e3.4. Distribution of average protein mutabilities for all human proteins in the 1 kG, genomAD and CKD patients\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eThe fig 6 presents the average distribution of proteins mutability shows that all amino acids proportionally exhibit higher mutability in genomAD dataset compared to 1 kg and CKD datasets and the average proteins mutability in CKD as well as in 1 kg are equally comparable. This higher mutability in genomAD is inherent to the gene fragments contained in this dataset as it harbors genomic variants as well as transcript variants.\u003c/p\u003e"},{"header":"Discussion","content":"\u003cp\u003eChronic kidney disease (CKD)\u0026nbsp;is defined as abnormalities in kidney structure or function and requires either GFR below 60 ml/min/1.73 m\u003csup\u003e2\u003c/sup\u003e or markers of kidney damage, including albuminuria [42]. It is a congruence of many vascular diseases with patients having dysfunctions of many physiological pathways. The pathology is infiltrated by other diseases like: diabetes, hypertension [43-45], cardiovascular morbidity [46, 47] as well as many genetic abnormalities like genomic instability [47, 48-51]and instability which is later translated into chromosomal damage and ultimately culminating to renal pathologies. Recent progress in genome-wide association studies revealed SNPs linked to different pathologies associated to CKD like: \u0026nbsp;hypertension [52], coronary artery disease [53], subclinical vascular disease [54] and overlapping between genetic variants observed in CKD patients and cardiovascular pathologies [55].\u003c/p\u003e\n\u003cp\u003e\u0026nbsp;The goal of our study is to establish a repertoire of allelic variants that are susceptible to kidney diseases and ultimately find some candidate genes directly linked to CKD. To this end, we run exome sequencing from CKD patient samples and determined the average mutation distribution sites within genomic regions from different variants. After bioinformatic analysis coupled with filtrations and hard filtrations, we came up with two single genes that are common to all patients (data not shown as we will be reporting this separately). We also derived the substitutions or exchanges between the amino acids, their mutabilities as well as the probabilistic distribution of these amino acid exchanges in human proteome. Our results from this study provides a unique relation between amino acids exchanges status in CKD. The results as presented on table 1 clearly show a statistically difference between some individual amino acids exchange matrix in CKD patients as compared with the natural variants, we derived from 1000 genome and genomAD datasets. Our data corroborate with those reported by De Beer et al [1] that the amino acids change in disease-associated variants differed radically from variants obtained from 1000 genome dataset. In this study, we went one step forward to establish a net difference in variation between amino acids exchanges deriving from CKD patients to those obtained from 1000 genome and genomAD datasets. This is a first demonstration as such in the scope of CKD patients using a square PAM matrix format 20 X 20 PAM to derive amino acids substitution and their plausible mutabilities in renal disease.\u0026nbsp;\u003c/p\u003e\n\u003cp\u003eIn the concept of mutability, it is also known that cytosines in a cytosine\u0026ndash;guanine (CpG) dinucleotide context is known for their propensity to mutate at a rate that can be several hundred-fold greater than transversions at other bases\u003cstrong\u003e,\u003c/strong\u003e and in genetic variation, these representations are disproportionately represented. It was shown that, hotspots regions of CpG dinucleotides islands play a role in mutational mechanism leading to determination of the amino acids that are prone to mutation. Our data in genomAD in term of mutability presents the same profile as well as the one from 1000 genome dataset as compared with CKD dataset where some cells in our table 1 present\u0026nbsp;statistically significant difference in term of exchangeability between the CKD patients\u0026rsquo; dataset. However,\u0026nbsp;the genomAD database shows a proportionally higher mutability for all amino acids compared to 1 kg and CKD datasets and the average proteins mutability in CKD as well as in 1 kg are equally comparable (fig 6). This difference in mutability is inherent to the nature of the three datasets. \u0026nbsp;First, we obtained the CKD dataset from Exome sequencing experiment on Illumina Platform. Then, the DNA sequencing we are dealing with stemmed from the transcripts although some primers from Illumina kits can sometime overlap with some intervening sequences and thereby introducing possibilities that some genomic sequence may be carried on in the results of sequencing data. Second, whereas the1000 genome database was developed using a combination of multiple sequencing approaches, including: low coverage whole genome sequencing, with depth mean of 7.4X, deep Exome sequencing with depth mean of 65.7X and dense microarray genotyping, the result in this database is believed to emanate from the transcript pools uniquely. Therefore, scientists use 1000 genome data base as reference to run variants for Exome sequencing data. \u0026nbsp;Lastly, the genomAD database in contrary was\u0026nbsp;developed by harmonizing both exome and genome sequencing data from a wide variety of large-scale sequencing projects, then it is a direct combination of Exome sequencing and whole genome sequencing data, and this may explain the higher proportion of mutability index score observed in this database comparatively to 1000 genome and CKD datasets. Moreover, on genomic scale, the human genome is known to contain\u0026nbsp;\u003cstrong\u003e\u0026sim;\u003c/strong\u003e\u003cstrong\u003e30,000 CpG islands\u003c/strong\u003e, long stretches (CpG repeats) of DNA and with unusually elevated levels of CpG dinucleotides with many occurring at genes promoters. \u0026nbsp;CpG islands are also residents of intervening sequences making the genes prone to mutation thus explaining their contribution to diseases. This also explains a higher distribution of average mutability in genomAD as compared with 1 kg and CKD as seen in fig 6. \u0026nbsp; In our experiment reported in (figure S1), we compared the number of mutations and the probabilistic distribution of amino acids in human proteome. We observed that Arginine (R) was the outlier with higher mutability index as compared to the rest of amino acids. \u0026nbsp;In fine, after the observation of the natural variants in genomAD as well as in 1000 genome databases, it is conclusive to say that the amino acids mutability is mostly driven by the nature and state of the DNA and the mutational mechanisms are favored at the codons harboring the CpG dinucleotides context and this explain why Arginine (R) mutates more than twice than other amino acids. This increase in Arginine (R) variants and mutability we observed in the three datasets\u0026nbsp;can be explained by the deamination of methylated cytosine (5mC) that is changed upon mutation into thymine, which is not readily detected by DNA repair systems.\u0026nbsp;Interestingly, Arginine (R) is the only amino acid to contain CpG dinucleotides at the first and second codon positions, which are less redundant than the third wobble position and therefore more likely to lead to an amino acid change. Moreover, Arginine (R) is encoded by six codons in vertebrate genomes with following features: four CGN codons (CGA, CGC, CGG, CGU) and two AGR codons (AGG, AGA). Base-pair changes in any of these codons can have a wide extensive range of effects in human genome, including: substitution of 12 different amino acids, two stop codons as well as eighteen synonymous mutations. Four amino acids, viz: Tryptophan, Histidine Glutamine and Cysteine account for 75% exchanges for arginine. This implies that the mechanism of selection purification or mutational bias is at work. The transitions of four (A \u0026gt; T and G \u0026gt;A) of six of arginine codons appear to be the drivers behind canonical mutation of arginine codons, a universal signature that independent of the origin of disease tissues. Indeed, recent studies have demonstrated that (A \u0026gt; T and G \u0026gt;A transitions are the causes of depletion of Arginine in human cancers [56]. Then, codon usage four CGN codons despite the hypermutability at CpG dinucleotides islands and the existence of AGR alternative codons, suggests the propensity of negative selective pressure directed toward these sites thereby amounting for the evolution of genetic code through Arginine bias mutation in from our CKD patients. Indeed, data archived in the database of clinically relevant variants (ClinVar) (57) revealed that arginine substitutions underlie 20.0% of all pathogenic single-nucleotide variants (SNVs), making arginine the most commonly substituted amino. The analysis of human genome has found that genes with coding regions of CGN arginine codons are present in higher proportion as compared with AGR arginine codons and CGN codons were enriched among disease genes and with strong correlation with measures of variance intolerance, an indication that, genes with CGN signatures preference are more likely to sustain single-genes mutation diseases (58). \u0026nbsp;\u003c/p\u003e\n\u003cp\u003eMoreover, data from thermodynamic experiments have reported that disease-causing variants have tendency to destabilize protein structures and their interactions [59, 60]. Later on, mutagenesis studies have also reported that replacing nonpolar group by polar ones can increase protein solubility. For example, on the study with RNase Sa, it was found that, the most buried carboxylic groups which are Asp33 (99% buried) and Asp79 (85% buried) and their respective mutants D33A mutants and D79A are 6kcal/mol and 3.3 kcal/mol less stable than the wild type [61, 62] and replacing Thr 76 by Asp acid increase the protein solubility [59]. In our current study, we noticed that four major amino acids, \u003cem\u003eviz\u003c/em\u003e: \u003cstrong\u003eTryptophan (W), Histidine (H), Glycine (G)\u003c/strong\u003e and \u003cstrong\u003eLysine (L)\u003c/strong\u003e have \u003cstrong\u003eArginine (R)\u003c/strong\u003e as common final common product of mutability. Whether this phenomenon is specifically peculiar to kidney diseases or widely observed features in biological arena, this remains to be investigated thoroughly via site-specific mutagenesis studies because each amino acid has its profile of physicochemical characteristic property and can therefore influence the final protein chemical structure. Nonetheless, this observation is the first we are reporting in kidney disease.\u003c/p\u003e\n\u003cp\u003eIt is also well documented that the determination of protein distances between many sequences necessitates the knowledge of the amino acids substitution rates [26] and invariably, the evolutionary pressure also depends on some amino acid physicochemical properties like isoelectric point, polarity and its volume [27]. We analyzed and compared the amino acids substitution rates between our three datasets and observed a strong positive correlation between the mutabilities as reported on fig 3 and (figure \u003cstrong\u003eS3\u003c/strong\u003e). This positive correlation demonstrates a close evolutionary distance between the proteins, at least from the three datasets we investigated: our CKD database, 1kg and genomAD database. During evolution, energetically favorable interaction is preserved and intra-protein remaining vicinities depend on the residual amino acids and unfavorable interaction are eliminated. Since it is generally accepted that more substitutions of amnio acids are needed to change one evolutionary sequence into another one and the more substitutions we have, the larger becomes the evolutionary distance [26 27], the substitution data we generated from the three-database correlate with the literature\u0026nbsp;\u003c/p\u003e"},{"header":"Conclusion","content":"\u003cp\u003eWe run Exome sequencing and established a PAM matrix of amino acids changes in CKD patients and compared this matrix to matrices obtained from 1000 genome and genomAD databases. The data demonstrated that the amino acids mutability index in CKD data was statistically significant different as compared with 1000 genome and genomAD datasets. There is strong positive correlation in mutabilities of amino acids distribution in human proteome and the average distribution of mutability is higher in genomAD dataset as compared CKD and 1000 genome. In the CKD dataset, Arginine remains a common product of mutability from four amino acids like: Tryptophan, Histidine, Glycine and Lysine and Arginine was shown to be also the outlier and the driver of mutability in the three data sets. More experiments remained to be conducted, more especially using other diseases context dataset to ascertain the peculiar mutability pattern of Arginine. Nonetheless, this study remains the first finding to layout clearly a profile of amino acids changes in CKD as well as a jump in mutability in genomAD dataset.\u003c/p\u003e"},{"header":"Declarations","content":"\u003cp\u003e\u003cstrong\u003e\u003cem\u003eEthics approval\u003c/em\u003e\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eThis study is part of a subgroup of an investigation started while ago on hemodialysis patients from outpatient\u0026rsquo;s clinics of King Khaled Hospital. The ethic approval committee issued patients\u0026rsquo; informed consent for participation authorization for publishing to Dr. Alaraj. [17-]and the subsequent four publications emanating from these patients were under the same authorization Dr. Alaraj who negotiated the blood samples.\u0026nbsp;\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e\u003cem\u003eAvailability of data and material\u003c/em\u003e\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eCKD patients\u0026rsquo; raw data: SNPs files, amino acids exchanges files as well as nucleotides interconversion are the authors property. These databases were generated by the authors for publication. Once they are published, the raw data can be shared with some credible scientists if they make a direct request to the corresponding author. 1000 genome natural variants were obtained from Ensembl [22] v67, as described in de Beer et al [1]. The natural variants from gnomAD dataset (v.2.0) were downloaded from the Broad Institute\u0026rsquo;s web site.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e\u003cem\u003eCompeting interests\u003c/em\u003e\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eAuthors declare no competing interests.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e\u003cem\u003eFundings\u003c/em\u003e\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eEdem Nuglozeh received in part financial support from The University of Hail in Saudi Arabia, and Hail City Kidney foundation.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e\u003cem\u003eAuthor contributions\u003c/em\u003e\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eAll authors contributed to the study conception and design. Material preparation, data collection and analysis were performed by [\u003cstrong\u003e\u003cem\u003eEdem Nuglozeh\u003c/em\u003e and \u003cem\u003eMohammad F. Fazaludeen\u003c/em\u003e\u003c/strong\u003e], [ \u003cstrong\u003eFatih Sağlam\u003c/strong\u003e] performed the graphic art work, organization of amino acids PAM matrix and statistics analysis. The first draft of the manuscript was written by [\u003cem\u003eEdem Nuglozeh\u003c/em\u003e] and all authors commented on previous versions of the manuscript. All authors read and approved the final manuscript for publication.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003e\u003cem\u003eAcknowledgements\u003c/em\u003e\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eThe authors are indebted to The University of Hail, School of Medicine as well as for Hail City Kidney foundation for the financial support of this work as well as European Bioinformatic Institute and McGill University, Department of Bioinformatics.\u0026nbsp;\u003c/p\u003e"},{"header":"References","content":"\u003col\u003e\n\u003cli\u003ede Beer TA, Laskowski RA, Parks SL, Sipos B, Goldman N, Thornton JM\u003cem\u003e.\u003c/em\u003e Amino Acid Changes in Disease-Associated Variants Differ Radically from Variants Observed in the 1000 Genomes Project Dataset. \u003cem\u003ePLoS Comput. Biol.\u003c/em\u003e 2013: \u003cstrong\u003e9(12):\u003c/strong\u003e e1003382\u003cstrong\u003e.\u003c/strong\u003e doi: 10.1371/journal.pcbi.1003382. Epub 2013 Dec 12. 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Biol.\u003c/em\u003e \u003cstrong\u003e354\u003c/strong\u003e, 967\u0026ndash;978 (2005).\u003c/li\u003e\n\u003c/ol\u003e"},{"header":"Tables","content":"\u003cp\u003e\u003cstrong\u003eTable 1. \u0026nbsp;Observation of amino acids exchanges in human proteins variants\u003c/strong\u003e\u003c/p\u003e\n\u003ctable style=\"border: none;width:109.0%;margin-left:-35.7pt;border-collapse:collapse;\"\u003e\n \u003ctbody\u003e\n \u003ctr\u003e\n \u003ctd rowspan=\"2\" style=\"width:6.68%;border:solid windowtext 1.0pt;border-bottom:solid black 1.0pt;padding:0cm 0cm 0cm 0cm;height:1.0pt;\"\u003e\n \u003cp style='margin-right:0cm;margin-left:0cm;font-size:15px;font-family:\"Calibri\",sans-serif;margin-top:0cm;margin-bottom:0cm;line-height:normal;text-align:center;'\u003e\u003cspan style='font-size:11px;font-family:\"Times New Roman\",serif;color:black;'\u003efrom\u003c/span\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd colspan=\"20\" style=\"width:84.76%;border-top:solid windowtext 1.0pt;border-left:none;border-bottom:solid windowtext 1.0pt;border-right:solid black 1.0pt;padding:0cm 0cm 0cm 0cm;height:1.0pt;\"\u003e\n \u003cp style='margin-right:0cm;margin-left:0cm;font-size:15px;font-family:\"Calibri\",sans-serif;margin-top:0cm;margin-bottom:0cm;line-height:normal;text-align:center;'\u003e\u003cspan style='font-size:11px;font-family:\"Times New Roman\",serif;color:black;'\u003eTo\u003c/span\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd rowspan=\"2\" style=\"width:4.88%;border-top:solid windowtext 1.0pt;border-left:none;border-bottom:solid black 1.0pt;border-right:solid windowtext 1.0pt;padding:0cm 0cm 0cm 0cm;height:1.0pt;\"\u003e\n \u003cp style='margin-right:0cm;margin-left:0cm;font-size:15px;font-family:\"Calibri\",sans-serif;margin-top:0cm;margin-bottom:0cm;line-height:normal;text-align:center;'\u003e\u003cspan style='font-size:11px;font-family:\"Times New Roman\",serif;color:black;'\u003eTotal\u003c/span\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd rowspan=\"2\" style=\"width:3.66%;border-top:solid windowtext 1.0pt;border-left:none;border-bottom:solid black 1.0pt;border-right:solid windowtext 1.0pt;padding:0cm 0cm 0cm 0cm;height:1.0pt;\"\u003e\n \u003cp style='margin-right:0cm;margin-left:0cm;font-size:15px;font-family:\"Calibri\",sans-serif;margin-top:0cm;margin-bottom:0cm;line-height:normal;text-align:center;'\u003e\u003cspan style='font-size:11px;font-family:\"Times New Roman\",serif;color:black;'\u003eMUT\u003c/span\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd style=\"width:4.32%;border-top:none;border-left:none;border-bottom:solid windowtext 1.0pt;border-right:solid windowtext 1.0pt;padding:0cm 0cm 0cm 0cm;height:1.0pt;\"\u003e\n \u003cp style='margin-right:0cm;margin-left:0cm;font-size:15px;font-family:\"Calibri\",sans-serif;margin-top:0cm;margin-bottom:0cm;line-height:normal;text-align:center;'\u003e\u003cspan style='font-size:11px;font-family:\"Times New Roman\",serif;color:black;'\u003eR\u003c/span\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd style=\"width:5.24%;border-top:none;border-left:none;border-bottom:solid windowtext 1.0pt;border-right:solid windowtext 1.0pt;padding:0cm 0cm 0cm 0cm;height:1.0pt;\"\u003e\n \u003cp style='margin-right:0cm;margin-left:0cm;font-size:15px;font-family:\"Calibri\",sans-serif;margin-top:0cm;margin-bottom:0cm;line-height:normal;text-align:center;'\u003e\u003cspan style='font-size:11px;font-family:\"Times New Roman\",serif;color:black;'\u003eK\u003c/span\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd style=\"width:3.56%;border-top:none;border-left:none;border-bottom:solid windowtext 1.0pt;border-right:solid windowtext 1.0pt;padding:0cm 0cm 0cm 0cm;height:1.0pt;\"\u003e\n \u003cp style='margin-right:0cm;margin-left:0cm;font-size:15px;font-family:\"Calibri\",sans-serif;margin-top:0cm;margin-bottom:0cm;line-height:normal;text-align:center;'\u003e\u003cspan style='font-size:11px;font-family:\"Times 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style='font-size:11px;font-family:\"Times New Roman\",serif;color:black;'\u003e249193\u003c/span\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd style=\"width:3.74%;border-top:none;border-left:none;border-bottom:solid windowtext 1.0pt;border-right:solid windowtext 1.0pt;padding:0cm 0cm 0cm 0cm;height:1.0pt;\"\u003e\n \u003cp style='margin-right:0cm;margin-left:0cm;font-size:15px;font-family:\"Calibri\",sans-serif;margin-top:0cm;margin-bottom:0cm;line-height:normal;text-align:center;'\u003e\u003cspan style='font-size:11px;font-family:\"Times New Roman\",serif;color:black;'\u003e94906\u003c/span\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd style=\"width:4.88%;border-top:none;border-left:none;border-bottom:solid windowtext 1.0pt;border-right:solid windowtext 1.0pt;padding:0cm 0cm 0cm 0cm;height:1.0pt;\"\u003e\n \u003cp style='margin-right:0cm;margin-left:0cm;font-size:15px;font-family:\"Calibri\",sans-serif;margin-top:0cm;margin-bottom:0cm;line-height:normal;text-align:center;'\u003e\u003cspan style='font-size:11px;font-family:\"Times New Roman\",serif;color:black;'\u003e4703947\u003c/span\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd style=\"width:3.66%;border-top:none;border-left:none;border-bottom:solid windowtext 1.0pt;border-right:solid windowtext 1.0pt;padding:0cm 0cm 0cm 0cm;height:1.0pt;\"\u003e\n \u003cp style='margin-right:0cm;margin-left:0cm;font-size:15px;font-family:\"Calibri\",sans-serif;margin-top:0cm;margin-bottom:0cm;line-height:normal;text-align:center;'\u003e\u003cspan style='font-size:11px;font-family:\"Times New Roman\",serif;color:black;'\u003e\u0026nbsp;\u003c/span\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003c/tbody\u003e\n\u003c/table\u003e\n\u003cp\u003eThe data in table 1 depicting the CKD patients on the top in the row of each cell, 1kG in the middle and genomAD in the bottom. Amino acids are arranged according to one single letter nomenclature following the scale of Fauch\u0026egrave;re and Pliska according to their increasing hydrophobicity from left to right and the top to the bottom. The less hydrophobic are on the left and the most on the right. The yellow blocks indicate absence of a statistically significant difference between the CKD patients and the two data sets, the light blue cells mean there is a statistically significant difference between the CKD patients data set and 1kG, genomAD or 1 kG and genomAD together. In the column representing the total number of mutations, the green color denotes absence of mutation between the CKD patients and the two data sets while the light brown color indicates presence of significant difference between the CKD patients and the two data sets.\u0026nbsp;\u003c/p\u003e"}],"fulltextSource":"","fullText":"","funders":[],"hasAdminPriorityOnWorkflow":false,"hasManuscriptDocX":true,"hasOptedInToPreprint":true,"hasPassedJournalQc":"","hasAnyPriority":false,"hideJournal":true,"highlight":"","institution":"","isAcceptedByJournal":false,"isAuthorSuppliedPdf":false,"isDeskRejected":"","isHiddenFromSearch":false,"isInQc":false,"isInWorkflow":false,"isPdf":false,"isPdfUpToDate":true,"isWithdrawnOrRetracted":false,"journal":{"display":true,"email":"[email protected]","identity":"researchsquare","isNatureJournal":false,"hasQc":true,"allowDirectSubmit":true,"externalIdentity":"","sideBox":"","snPcode":"","submissionUrl":"/submission","title":"Research Square","twitterHandle":"researchsquare","acdcEnabled":true,"dfaEnabled":false,"editorialSystem":"","reportingPortfolio":"","inReviewEnabled":false,"inReviewRevisionsEnabled":true},"keywords":"CKD, PAM Matrix, Amino Acids, Mutability","lastPublishedDoi":"10.21203/rs.3.rs-4268762/v1","lastPublishedDoiUrl":"https://doi.org/10.21203/rs.3.rs-4268762/v1","license":{"name":"CC BY 4.0","url":"https://creativecommons.org/licenses/by/4.0/"},"manuscriptAbstract":"\u003cp\u003e\u003cem\u003e\u003cstrong\u003eBackground:\u003c/strong\u003e\u003c/em\u003e Nonsynonymous mutations in the coding regions of human genes are responsible for phenotypic differences between humans and for their susceptibility to genetic disease.\u003c/p\u003e\n\u003cp\u003e\u003cem\u003e\u003cstrong\u003eMethods:\u003c/strong\u003e\u003c/em\u003e\u003cstrong\u003e \u003c/strong\u003eWe performed Exome sequencing on CKD patients’ genomic DNA and put the focus in understanding the role played by the amino-acid mutation spectrum (PAM) in human chronic kidney disease CKD patients. More specifically, using SIFT algorithm, we generated the amino acids substitution on proteins and compared the PAM matrix derived from CKD patients representing the amino-acid mutational spectrum to non-disease PAM matrices representing spectra of mutual amino-acid mutation frequencies derived from 1000 genome and genomAD database.\u003c/p\u003e\n\u003cp\u003e\u003cem\u003e\u003cstrong\u003eResults:\u003c/strong\u003e\u003c/em\u003e \u003cstrong\u003e\u0026nbsp;\u003c/strong\u003eWe found a strong and positive correlation in term of mutabilities of amino acids distribution in human proteome and the average distribution of amino acid mutability remains higher in genomAD dataset as compared CKD and 1000 genome. The results also show a strong correlation of mutability between the three datasets, the coefficient of correlation being: (\u003cstrong\u003er\u003c/strong\u003e\u003csub\u003e\u003cstrong\u003eCKD vs 1kg \u003c/strong\u003e\u003c/sub\u003e\u003cstrong\u003e=\u003c/strong\u003e\u003csub\u003e\u003cstrong\u003e \u003c/strong\u003e\u003c/sub\u003e\u003cstrong\u003e0.9225\u003c/strong\u003e\u003csub\u003e\u003cstrong\u003e, \u003c/strong\u003e\u003c/sub\u003e\u003cstrong\u003er\u003c/strong\u003e\u003csub\u003e\u003cstrong\u003eCKD vs genomAD \u003c/strong\u003e\u003c/sub\u003e\u003cstrong\u003e= 0.943\u003c/strong\u003e1 and \u003cstrong\u003er\u003c/strong\u003e\u003csub\u003e\u003cstrong\u003egenomAD vs 1kg\u003c/strong\u003e\u003c/sub\u003e\u003cstrong\u003e = 0.9486\u003c/strong\u003e) as well probabilistic distribution of amino acids in human proteome between the three datasets.\u003c/p\u003e\n\u003cp\u003e\u003cem\u003e\u003cstrong\u003eConclusion:\u003c/strong\u003e\u003c/em\u003e\u003cstrong\u003e \u003c/strong\u003eThe amino acids mutability \u003cem\u003eindex\u003c/em\u003e in CKD dataset was statistically different as compared with those in 1000 genome and genomAD datasets. There is strong positive correlation in mutabilities of amino acids distribution in human proteome and the average distribution of mutability is higher in genomAD dataset as compared CKD and 1000 genome. In the CKD dataset, \u003cem\u003eArginine\u003c/em\u003e remains a common product of mutability from four amino acids like: \u003cem\u003eTryptophan, Histidine, Glycine\u003c/em\u003e and \u003cem\u003eLysine\u003c/em\u003e and the spike of Arginine in blood samples should be an element to trace in diagnostic profile of CKD. The data paved a way for clinical use for amino acids exchanges in chronic kidney disease using Illumina platform.\u003c/p\u003e","manuscriptTitle":"Amino acids exchange obtained from CKD patients via Exome Sequencing differ radically from those of natural variants 1000 genome and genomAD databases","msid":"","msnumber":"","nonDraftVersions":[{"code":1,"date":"2024-04-30 19:43:53","doi":"10.21203/rs.3.rs-4268762/v1","editorialEvents":[{"type":"communityComments","content":0}],"status":"published","journal":{"display":true,"email":"[email protected]","identity":"researchsquare","isNatureJournal":false,"hasQc":true,"allowDirectSubmit":true,"externalIdentity":"","sideBox":"","snPcode":"","submissionUrl":"/submission","title":"Research Square","twitterHandle":"researchsquare","acdcEnabled":true,"dfaEnabled":false,"editorialSystem":"","reportingPortfolio":"","inReviewEnabled":false,"inReviewRevisionsEnabled":true}}],"origin":"","ownerIdentity":"34a1cb60-c230-4112-97cc-207e46a69eea","owner":[],"postedDate":"April 30th, 2024","published":true,"recentEditorialEvents":[],"rejectedJournal":[],"revision":"","amendment":"","status":"posted","subjectAreas":[],"tags":[],"updatedAt":"2025-06-12T15:53:23+00:00","versionOfRecord":[],"versionCreatedAt":"2024-04-30 19:43:53","video":"","vorDoi":"","vorDoiUrl":"","workflowStages":[]},"version":"v1","identity":"rs-4268762","journalConfig":"researchsquare"},"__N_SSP":true},"page":"/article/[identity]/[[...version]]","query":{"redirect":"/article/rs-4268762","identity":"rs-4268762","version":["v1"]},"buildId":"qtupq5eGEP_6zYnWcrvyt","isFallback":false,"isExperimentalCompile":false,"dynamicIds":[84888],"gssp":true,"scriptLoader":[]}