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A glycan cluster on the SARS-CoV-2 spike ectodomain is recognized by Fab-dimerized glycan-reactive antibodies

By Priyamvada Acharya, Wilton Williams, Rory Henderson, Katarzyna Janowska, Kartik Manne, Robert Parks, Margaret Deyton, Jordan Sprenz, Victoria Stalls, Megan Kopp, Katayoun Mansouri, Robert J Edwards, R. Ryan Meyerhoff, Thomas Oguin, Gregory Sempowski, Kevin Saunders, Barton F Haynes

Posted 30 Jun 2020
bioRxiv DOI: 10.1101/2020.06.30.178897

The COVID-19 pandemic caused by SARS-CoV-2 has escalated into a global crisis. The spike (S) protein that mediates cell entry and membrane fusion is the current focus of vaccine and therapeutic antibody development efforts. The S protein, like many other viral fusion proteins such as HIV-1 envelope (Env) and influenza hemagglutinin, is glycosylated with both complex and high mannose glycans. Here we demonstrate binding to the SARS-CoV-2 S protein by a category of Fab-dimerized glycan-reactive (FDG) HIV-1-induced broadly neutralizing antibodies (bnAbs). A 3.1 Å resolution cryo-EM structure of the S protein ectodomain bound to glycan-dependent HIV-1 bnAb 2G12 revealed a quaternary glycan epitope on the spike S2 domain involving multiple protomers. These data reveal a new epitope on the SARS-CoV-2 spike that can be targeted for vaccine design. ### Competing Interest Statement The authors have declared no competing interest.

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