Role of the C-terminal Modules of Klebsiella Phage KP32 Receptor-Binding Protein gp38 in Protein and Phage Functionality

Role of the C-terminal Modules of Klebsiella Phage KP32 Receptor-Binding Protein gp38 in Protein and Phage Functionality | 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 Article Role of the C-terminal Modules of Klebsiella Phage KP32 Receptor-Binding Protein gp38 in Protein and Phage Functionality Agnieszka Latka, Dorien Dams, Lennert Scholiers, Aleksandra Otwinowska, and 3 more This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-5986232/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 Despite significant progress in understanding phage biology and their clinical applications, the specificity of phages remains only merely understood and a matter of empirical testing. This study investigates the receptor-binding protein KP32gp38 of Klebsiella phage KP32, which features a unique C-terminal tandem of a carbohydrate-binding module (CBM) and a lectin-like (LEC) domain. We dissected the roles of these modules in trimerization, substrate binding, and specificity. Our results demonstrate that the LEC domain is essential for trimerization, while the CBM domain is crucial for enzymatic activity and capsule binding. Engineered phages lacking these domains confirmed the necessity of both CBM and LEC for full functionality. This work underscores the versatility and evolutionary adaptation of CBM and LEC folds in phage RBPs, providing valuable insights into phage specificity mechanisms. Our findings offer a blueprint for understanding the molecular determinants of phage-host interactions, crucial for advancing phage-based antibacterial therapies. Biological sciences/Microbiology/Bacteriophages Biological sciences/Microbiology/Phage biology Biological sciences/Biotechnology/Molecular engineering/Synthetic biology Klebsiella phage specificity receptor-binding protein depolymerase tailspike carbohydrate-binding module lectin-like domain Full Text Additional Declarations There is NO Competing Interest. Supplementary Files SupplementarymaterialsLatkaetal.xlsx Supplementary materials 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. 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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-5986232","acceptedTermsAndConditions":true,"allowDirectSubmit":true,"archivedVersions":[],"articleType":"Article","associatedPublications":[],"authors":[{"id":417052837,"identity":"375ba358-0adb-4aad-9b6b-bfe6fe84d7be","order_by":0,"name":"Agnieszka Latka","email":"","orcid":"https://orcid.org/0000-0003-4492-497X","institution":"Department of Biotechnology, Ghent University, Ghent, Belgium; Department of Pathogen Biology and Immunology, University of Wroclaw, Wroclaw, 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