The D614G mutation in the SARS-CoV-2 spike protein reduces S1 shedding and increases infectivity
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Preprint
- 12 June 2020
- preprint
- Published by Cold Spring Harbor Laboratory in bioRxiv
Abstract
SARS coronavirus 2 (SARS-CoV-2) isolates encoding a D614G mutation in the viral spike (S) protein predominate over time in locales where it is found, implying that this change enhances viral transmission. We therefore compared the functional properties of the S proteins with aspartic acid (SD614) and glycine (SG614) at residue 614. We observed that retroviruses pseudotyped with SG614infected ACE2-expressing cells markedly more efficiently than those with SD614. This greater infectivity was correlated with less S1 shedding and greater incorporation of the S protein into the pseudovirion. Similar results were obtained using the virus-like particles produced with SARS-CoV-2 M, N, E, and S proteins. However, SG614did not bind ACE2 more efficiently than SD614, and the pseudoviruses containing these S proteins were neutralized with comparable efficiencies by convalescent plasma. These results show SG614is more stable than SD614, consistent with epidemiological data suggesting that viruses with SG614transmit more efficiently.Keywords
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- Published version: Nature Communications, 11 (1), 1.
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