Analysis of Siderophore Acyltransferase SidL protein of Aspergillus fumigatus

Analysis of Siderophore Acyltransferase SidL protein of Aspergillus fumigatus | 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 Analysis of Siderophore Acyltransferase SidL protein of Aspergillus fumigatus Rasha M.A. Al-Humairi, Osama Abdulmunem K., Ali M.Hussein, Mohammed I. Jameel, and 2 more This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-7947990/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: Aspergillus fumigatus is a leading opportunistic filamentous fungal pathogen whose capacity to secrete hydroxamate siderophores is central to iron acquisition, the oxidative stress response and virulence. One of the key enzymes, SidL is required for the biosynthesis of ferricrocin and hydroxyferricrocin but has never been structurally characterized. In the present study, various silico analyses were conducted to elucidate physicochemical properties, subcellular localization, secondary structure, homology model validation and protein-protein interaction network of SidL. Methods: Uniprot was used to obtain the monoacid sequence, and Expasy's ProtParam tool was used to predict physicochemical properties. The DeepLoc-2.0 was used for protein's subcellular location, InterProScan for function prediction, and PSIPRED and SOPMA for the secondary structure. SWISS-MODEL was utilized to predict the three-dimensional structure, the STRING database for protein-protein interactions, and finally, the DoGSiteScorer and FTSite for checking the Draggability and Binding Site. Results: ProtParam showed that the protein is hydrophobic and unstable with 484 amino acids, predicted molecular weight of ~54.8 kDa. Its subcellular localization was predicted as cytoplasmic, and secondary structure analysis showed it to be rich in α-helices. 3D structural model was generated by homology modeling using SWISS-MODEL and validated by SAVES quality assessment. The string analyses showed potential functional interactions with other siderophore biosynthesis enzymes and doGSiteScorer and FTSite identified a draggable binding pocket that received promising scores. Conclusions: This study presents the first comprehensive computational characterization of SidL, a siderophore acyltransferase from Aspergillus fumigatus. By highlighting SidL’s potential draggability, this work supports its consideration as a promising antifungal target, especially considering rising antifungal resistance and the urgent need for new therapeutic strategies. Aspergillus fumigatus Siderophore SidL In Silico Analysis Protein Characterization Full Text Additional Declarations No competing interests reported. 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-7947990","acceptedTermsAndConditions":true,"allowDirectSubmit":true,"archivedVersions":[],"articleType":"Research Article","associatedPublications":[],"authors":[{"id":538773095,"identity":"b689f996-0369-4370-8e0f-cae6408bf4d3","order_by":0,"name":"Rasha M.A. Al-Humairi","email":"","orcid":"","institution":"University of Baghdad","correspondingAuthor":false,"prefix":"","firstName":"Rasha","middleName":"M.A.","lastName":"Al-Humairi","suffix":""},{"id":538773096,"identity":"288edbb7-fa38-45fd-b2db-50f3782c9b98","order_by":1,"name":"Osama Abdulmunem K.","email":"","orcid":"","institution":"Al-Bayan University","correspondingAuthor":false,"prefix":"","firstName":"Osama","middleName":"Abdulmunem","lastName":"K.","suffix":""},{"id":538773097,"identity":"a2f6d246-161d-4087-9885-973fb83b95bc","order_by":2,"name":"Ali M.Hussein","email":"data:image/png;base64,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","orcid":"","institution":"Koya University","correspondingAuthor":true,"prefix":"","firstName":"Ali","middleName":"","lastName":"M.Hussein","suffix":""},{"id":538773098,"identity":"2ce0b343-a457-45dc-8d44-8b527ce3573e","order_by":3,"name":"Mohammed I. 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fumigatus","fulltext":[],"fulltextSource":"","fullText":"","funders":[],"hasAdminPriorityOnWorkflow":false,"hasManuscriptDocX":false,"hasOptedInToPreprint":true,"hasPassedJournalQc":"","hasAnyPriority":true,"hideJournal":true,"highlight":"","institution":"","isAcceptedByJournal":false,"isAuthorSuppliedPdf":true,"isDeskRejected":"","isHiddenFromSearch":false,"isInQc":false,"isInWorkflow":false,"isPdf":true,"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":"Aspergillus fumigatus, Siderophore, SidL, In Silico Analysis, Protein Characterization","lastPublishedDoi":"10.21203/rs.3.rs-7947990/v1","lastPublishedDoiUrl":"https://doi.org/10.21203/rs.3.rs-7947990/v1","license":{"name":"CC BY 4.0","url":"https://creativecommons.org/licenses/by/4.0/"},"manuscriptAbstract":"\u003cp\u003eBackground: Aspergillus fumigatus is a leading opportunistic filamentous fungal pathogen whose capacity to secrete hydroxamate siderophores is central to iron acquisition, the oxidative stress response and virulence. One of the key enzymes, SidL is required for the biosynthesis of ferricrocin and hydroxyferricrocin but has never been structurally characterized. In the present study, various silico analyses were conducted to elucidate physicochemical properties, subcellular localization, secondary structure, homology model validation and protein-protein interaction network of SidL.\u0026nbsp;\u003c/p\u003e\n\u003cp\u003eMethods: Uniprot was used to obtain the monoacid sequence, and Expasy's ProtParam tool was used to predict physicochemical properties. The DeepLoc-2.0 was used for protein's subcellular location, InterProScan for function prediction, and PSIPRED and SOPMA for the secondary structure. SWISS-MODEL was utilized to predict the three-dimensional structure, the STRING database for protein-protein interactions, and finally, the DoGSiteScorer and FTSite for checking the Draggability and Binding Site.\u0026nbsp;\u003c/p\u003e\n\u003cp\u003eResults: ProtParam showed that the protein is hydrophobic and unstable with 484 amino acids, predicted molecular weight of ~54.8 kDa. Its subcellular localization was predicted as cytoplasmic, and secondary structure analysis showed it to be rich in α-helices. 3D structural model was generated by homology modeling using SWISS-MODEL and validated by SAVES quality assessment. The string analyses showed potential functional interactions with other siderophore biosynthesis enzymes and doGSiteScorer and FTSite identified a draggable binding pocket that received promising scores.\u0026nbsp;\u003c/p\u003e\n\u003cp\u003eConclusions: This study presents the first comprehensive computational characterization of SidL, a siderophore acyltransferase from Aspergillus fumigatus. By highlighting SidL’s potential draggability, this work supports its consideration as a promising antifungal target, especially considering rising antifungal resistance and the urgent need for new therapeutic strategies.\u003c/p\u003e","manuscriptTitle":"Analysis of Siderophore Acyltransferase SidL protein of Aspergillus fumigatus","msid":"","msnumber":"","nonDraftVersions":[{"code":1,"date":"2025-11-04 05:47:48","doi":"10.21203/rs.3.rs-7947990/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":"4f6c2baf-45c3-481d-8701-a83ca28d1b51","owner":[],"postedDate":"November 4th, 2025","published":true,"recentEditorialEvents":[],"rejectedJournal":[],"revision":"","amendment":"","status":"posted","subjectAreas":[],"tags":[],"updatedAt":"2025-11-19T16:23:09+00:00","versionOfRecord":[],"versionCreatedAt":"2025-11-04 05:47:48","video":"","vorDoi":"","vorDoiUrl":"","workflowStages":[]},"version":"v1","identity":"rs-7947990","journalConfig":"researchsquare"},"__N_SSP":true},"page":"/article/[identity]/[[...version]]","query":{"redirect":"/article/rs-7947990","identity":"rs-7947990","version":["v1"]},"buildId":"8U1c8b4HqxoKbykW_rLl7","isFallback":false,"isExperimentalCompile":false,"dynamicIds":[84888],"gssp":true,"scriptLoader":[]}