Lactylation Dynamics in Myxozoan Proteins | 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 Lactylation Dynamics in Myxozoan Proteins Amr A. G. Ibrahim, Juliana Naldoni, Antônio A. M. Maia, Juliano R. Sangalli, and 5 more This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-9266461/v1 This work is licensed under a CC BY 4.0 License Status: Under Revision Version 1 posted 11 You are reading this latest preprint version Abstract Lactylation has recently emerged as a novel post-translational modification with critical implications for gene regulation and host–parasite interactions, as demonstrated in species of Plasmodium and Trypanosoma . Here, we applied an integrative approach combining in-silico predictive and experimental analyses to detect protein lactylation in parasitic cnidarians in the class Myxozoa. In-silico analyses were conducted using data from seven myxozoan species, six obtained from public databases and one generated in this study. Experimental validation was based on Oxford Nanopore Technologies (ONT) genome sequencing and Western blotting of Myxobolus macroplasmodialis samples. This integrative approach enabled us to validate the in-silico analysis, to identify conserved lactylation sites in key stress-response proteins (including HSP70 and several metabolic enzymes), and to map electrochemical signatures of lactylation sites in the ONT data for M. macroplasmodialis. Comparative analyses across species, supported by functional enrichment and network-based approaches, demonstrated conserved regulatory roles of lactylation alongside species-specific variation in the biological processes it controls. Functional enrichment analyses further implicated lactylation in critical pathways, including glycolysis, oxidative phosphorylation, and immune signaling, supporting its integration into core regulatory networks underlying the functional biology of parasitism. Myxozoa Epigenetics Oxford Nanopore sequencing Host–parasite interactions Cnidaria Full Text Additional Declarations No competing interests reported. Supplementary Files SuplementaryFigureS1.pdf SupplementaryFileS1.docx SupplementaryFileS2.docx SupplementaryFileS3.docx SupplementaryFileS4.docx SupplementaryFileS5.docx SupplementaryFileS6.docx SupplementaryTableS1.xlsx SupplementaryTableS2.xlsx Cite Share Download PDF Status: Under Revision Version 1 posted Editorial decision: Revision requested 30 Apr, 2026 Reviews received at journal 28 Apr, 2026 Reviews received at journal 25 Apr, 2026 Reviewers agreed at journal 13 Apr, 2026 Reviewers agreed at journal 13 Apr, 2026 Reviewers agreed at journal 10 Apr, 2026 Reviewers invited by journal 10 Apr, 2026 Editor assigned by journal 10 Apr, 2026 Editor invited by journal 10 Apr, 2026 Submission checks completed at journal 08 Apr, 2026 First submitted to journal 08 Apr, 2026 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-9266461","acceptedTermsAndConditions":true,"allowDirectSubmit":false,"archivedVersions":[],"articleType":"Research Article","associatedPublications":[],"authors":[{"id":624700992,"identity":"255b1977-96a4-4181-b698-49c8bccf14ac","order_by":0,"name":"Amr A. G. 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