Bovine ultralong complementarity-determining region H3 found to cross-react with Sarbecoviruses UniversityLeeds Sarbecovirus Coronaviruses CrossReact
By Pooja Toshniwal PahariaOct 24 2022Reviewed by Aimee Molineux In a recent study published in the Journal of Biological Chemistry, researchers performed an in vitro analysis to isolate ultralong bovine heavy chains that showed binding with severe acute respiratory syndrome coronavirus 2 and related coronaviruses .
A mammalian cell-surface screen was used for screening ultralong CDRH3 Ab libraries. Leukocyte gDNA variable exons of cows were amplified to generate an ultralong bovine paratope library. Subsequently, enrichment of the ultralong CDRH3 regions was performed by polymerase chain reaction and selection of sizes, for producing a library with ultralong CDRH3s.
Results Genetics & Genomics eBook Compilation of the top interviews, articles, and news in the last year. Download a copy today A broadly reactive and an ultralong scFv CDRH3 epitope was isolated from a SARS-CoV-2-naïve heavy-chain library that showed binding to SARS-CoV-2 RBD, all SARS-CoV-2 variants of concern and SARS-CoV RBD. The epitope neutralized SARS-CoV S-pseudotyped viruses, but not by competing with the ACE2 receptor binding.
Cells that transiently expressed B9-scFv showed binding to S, RBD and S1, but not with S2, indicating that the B9-scFv binding site was localized to RBD amino acid residue 319 to residue 591. The binding of B9-scFv to S protein-transfected cells was concentration-dependent and enriched compared to ultralong scFv controls.
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