Enzymatization of mouse monoclonal antibody to the corresponding catalytic antibody

Enzymatization of mouse monoclonal antibody to the corresponding catalytic antibody | 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 Enzymatization of mouse monoclonal antibody to the corresponding catalytic antibody Emi Hifumi, Yuina Ito, Moe Tsujita, Hiroaki Taguchi, Taizo Uda This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-3847195/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 Catalytic antibodies exhibit unique features for recognizing and degrading antigens. However, the production of these antibodies is time-consuming and labor-intensive. Herein, mouse monoclonal antibodies (mAbs) were converted into catalytic antibodies by deleting Pro95 in the light chain using three antibodies targeting the influenza A virus. Although no catalytic activity was observed for the mAbs and light chains, Pro95-deleted light chains exhibited catalytic activity for cleaving the antigenic peptide. The affinity of the Pro95-deleted light chains for the antigen increased approximately 100-fold compared to that of the wild-type light chains. Notably, the Pro95-deleted mutants suppressed influenza virus infection in the in vitro assay. Molecular modeling suggested that three residues (Asp1, Ser92, and His93) in the mutant moved closer to the appropriate position, enhancing catalytic function and immunoreactivity. Note that a rapid and simple method for generating catalytic antibodies for various diagnostic and therapeutic applications from exiting antibodies were attained. Biological sciences/Biochemistry/Biocatalysis Biological sciences/Biochemistry Monoclonal antibody Influenza virus Hemagglutinin Catalytic antibody Förster resonance energy transfer substrate Full Text Additional Declarations There is NO Competing Interest. Supplementary Files SupplementaryInformation.pdf Supplementary Figures 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-3847195","acceptedTermsAndConditions":true,"allowDirectSubmit":true,"archivedVersions":[],"articleType":"Article","associatedPublications":[],"authors":[{"id":268823421,"identity":"5ae9f700-0530-46c8-ae21-d73458a7ed2f","order_by":0,"name":"Emi 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