Structural Basis for Potent Neutralization of Betacoronaviruses by Single-Domain Camelid Antibodies.

Clicks: 322
ID: 106256
2020
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Abstract
Coronaviruses make use of a large envelope protein called spike (S) to engage host cell receptors and catalyze membrane fusion. Because of the vital role that these S proteins play, they represent a vulnerable target for the development of therapeutics. Here, we describe the isolation of single-domain antibodies (VHHs) from a llama immunized with prefusion-stabilized coronavirus spikes. These VHHs neutralize MERS-CoV or SARS-CoV-1 S pseudotyped viruses, respectively. Crystal structures of these VHHs bound to their respective viral targets reveal two distinct epitopes, but both VHHs interfere with receptor binding. We also show cross-reactivity between the SARS-CoV-1 S-directed VHH and SARS-CoV-2 S and demonstrate that this cross-reactive VHH neutralizes SARS-CoV-2 S pseudotyped viruses as a bivalent human IgG Fc-fusion. These data provide a molecular basis for the neutralization of pathogenic betacoronaviruses by VHHs and suggest that these molecules may serve as useful therapeutics during coronavirus outbreaks.
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wrapp2020structuralcell Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Wrapp, Daniel;De Vlieger, Dorien;Corbett, Kizzmekia S;Torres, Gretel M;Wang, Nianshuang;Van Breedam, Wander;Roose, Kenny;van Schie, Loes;, ;Hoffmann, Markus;Pöhlmann, Stefan;Graham, Barney S;Callewaert, Nico;Schepens, Bert;Saelens, Xavier;McLellan, Jason S;
Journal Cell
Year 2020
DOI
S0092-8674(20)30494-3
URL
Keywords
mers nanobody sars covid-19 sars-cov-2

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