Abstract

Event Abstract Back to Event Antigenization of bovine immunoglobulin variable regions for development of novel vaccines Yfke Pasman1 and Azad K. Kaushik1* 1 University of Guelph, Molecular and Cellular Biology, Canada Immunoglobulin specificity and affinity is a function of the complementarity determining regions (CDRs) of the heavy and light chain variable regions. The CDRs interact with the antigen as they stick out of the beta-sheets formed by the framework regions. The CDRs as such are stable conformational structures of an Immunoglobulin. The molecular modeling of bovine heavy (VH) and light (VL) chain domains predicted that the VL might only have a supportive role in antigen recognition in antibodies with exceptionally long CDR3H (>48 amino acids). It was hypothesized that bovine CDR3H could form the site for presentation of conformational B-cell epitopes in order to develop a vaccine. We have now expressed bovine VH with a CDR3H of 61 amino-acids and VL, as single chain variable fragment (scFv) with an 18 amino acid linker in Pichia pastoris. This scFv retained the (poly)specificity of the parent antibody in ELISA. This confirmed the conformational stability of the CDR3H region in this format. Previously a protein fragment containing a bovine herpesvirus-1 (BoHV-1) neutralizing epitope was identified in our laboratory. The sequence encoding this fragment will be grafted into the CDR3H encoding sequence and expressed as scFv in Pichia pastoris. Confirmation of the epitope structure will be done in ELISA with recombinant scFv3-18L against BoHV-1, previously engineered in our laboratory and in vivo testing in a BoHV-1 susceptible host. Antigenization of recombinant bovine antibody fragments could provide a novel approach to develop safe targeted vaccines. Acknowledgements Supported by NSERC Canada and the Dairy Farmers of Ontario Keywords: bovine, immunoglobulin, CDR3H, Antigenization, vaccine development Conference: 15th International Congress of Immunology (ICI), Milan, Italy, 22 Aug - 27 Aug, 2013. Presentation Type: Abstract Topic: Translational immunology and immune intervention Citation: Pasman Y and Kaushik AK (2013). Antigenization of bovine immunoglobulin variable regions for development of novel vaccines. Front. Immunol. Conference Abstract: 15th International Congress of Immunology (ICI). doi: 10.3389/conf.fimmu.2013.02.01176 Copyright: The abstracts in this collection have not been subject to any Frontiers peer review or checks, and are not endorsed by Frontiers. They are made available through the Frontiers publishing platform as a service to conference organizers and presenters. The copyright in the individual abstracts is owned by the author of each abstract or his/her employer unless otherwise stated. Each abstract, as well as the collection of abstracts, are published under a Creative Commons CC-BY 4.0 (attribution) licence (https://creativecommons.org/licenses/by/4.0/) and may thus be reproduced, translated, adapted and be the subject of derivative works provided the authors and Frontiers are attributed. For Frontiers’ terms and conditions please see https://www.frontiersin.org/legal/terms-and-conditions. Received: 30 Jul 2013; Published Online: 22 Aug 2013. * Correspondence: Dr. Azad K Kaushik, University of Guelph, Molecular and Cellular Biology, Guelph, Ontario, N1G 2W1, Canada, akaushik@uoguelph.ca Login Required This action requires you to be registered with Frontiers and logged in. To register or login click here. Abstract Info Abstract The Authors in Frontiers Yfke Pasman Azad K Kaushik Google Yfke Pasman Azad K Kaushik Google Scholar Yfke Pasman Azad K Kaushik PubMed Yfke Pasman Azad K Kaushik Related Article in Frontiers Google Scholar PubMed Abstract Close Back to top Javascript is disabled. Please enable Javascript in your browser settings in order to see all the content on this page.

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.