Author: Liu, Hejun; Wu, Nicholas C.; Yuan, Meng; Bangaru, Sandhya; Torres, Jonathan L.; Caniels, Tom G.; Schooten, Jelle van; Zhu, Xueyong; Lee, Chang-Chun D.; Brouwer, Philip J.M.; Gils, Marit J. van; Sanders, Rogier W.; Ward, Andrew B.; Wilson, Ian A.
Title: Cross-neutralization of a SARS-CoV-2 antibody to a functionally conserved site is mediated by avidity Cord-id: ul602otg Document date: 2020_8_3
ID: ul602otg
Snippet: Most antibodies isolated from COVID-19 patients are specific to SARS-CoV-2. COVA1-16 is a relatively rare antibody that also cross-neutralizes SARS-CoV. Here we determined a crystal structure of COVA1-16 Fab with the SARS-CoV-2 RBD, and a negative-stain EM reconstruction with the spike glycoprotein trimer, to elucidate the structural basis of its cross-reactivity. COVA1-16 binds a highly conserved epitope on the SARS-CoV-2 RBD, mainly through a long CDR H3, and competes with ACE2 binding due to
Document: Most antibodies isolated from COVID-19 patients are specific to SARS-CoV-2. COVA1-16 is a relatively rare antibody that also cross-neutralizes SARS-CoV. Here we determined a crystal structure of COVA1-16 Fab with the SARS-CoV-2 RBD, and a negative-stain EM reconstruction with the spike glycoprotein trimer, to elucidate the structural basis of its cross-reactivity. COVA1-16 binds a highly conserved epitope on the SARS-CoV-2 RBD, mainly through a long CDR H3, and competes with ACE2 binding due to steric hindrance rather than epitope overlap. COVA1-16 binds to a flexible up conformation of the RBD on the spike and relies on antibody avidity for neutralization. These findings, along with structural and functional rationale for the epitope conservation, provide a blueprint for development of more universal SARS-like coronavirus vaccines and therapies.
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