A Cryptic Site of Vulnerability on the Receptor Binding Domain of the SARS-CoV-2 Spike Glycoprotein
M. Gordon Joyce, Rajeshwer S Sankhala, Wei-Hung Chen, Misook Choe, Hongjun Bai, Agnes Hajduczki, Lianying Yan, Spencer L Sterling, Caroline Peterson, Ethan C Green, Clayton Smith, Natalia de Val, Mihret Amare, Paul Scott, Eric D Laing, Christopher C Broder, Morgane Rolland, Nelson L Michael, Kayvon Modjarrad
doi: https://doi.org/10.1101/2020.03.15.992883
Abstract
SARS-CoV-2 is a zoonotic virus that has caused a pandemic of severe respiratory disease—COVID-19—within several months of its initial identification. Comparable to the first SARS-CoV, this coronaviruses surface Spike (S) glycoprotein mediates cell entry via the human ACE-2 receptor, and, thus, is the principal target for the development of vaccines and immunotherapeutics. Molecular information on the SARS-CoV-2 S glycoprotein remains limited. Here we report the crystal structure of the SARS-CoV-2 S receptor-binding-domain (RBD) at a the highest resolution to date, of 1.95 Å. We identified a set of SARS-reactive monoclonal antibodies with cross-reactivity to SARS-CoV-2 RBD and other betacoronavirus S glycoproteins.
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