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The D614G mutation in the SARS-CoV-2 spike protein reduces S1 shedding and increases infectivity

Lizhou Zhang, Cody B Jackson, Huihui Mou, Amrita Ojha, Erumbi S Rangarajan, Tina Izard, Michael Farzan, Hyeryun Choe
doi: https://doi.org/10.1101/2020.06.12.148726
Lizhou Zhang
1Department of Immunology and Microbial Science, The Scripps Research Institute, Jupiter, FL 33458, USA
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Cody B Jackson
1Department of Immunology and Microbial Science, The Scripps Research Institute, Jupiter, FL 33458, USA
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Huihui Mou
1Department of Immunology and Microbial Science, The Scripps Research Institute, Jupiter, FL 33458, USA
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Amrita Ojha
1Department of Immunology and Microbial Science, The Scripps Research Institute, Jupiter, FL 33458, USA
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Erumbi S Rangarajan
2Department of Integrative Structural and Computational Biology, The Scripps Research Institute, Jupiter, Florida 33458
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Tina Izard
2Department of Integrative Structural and Computational Biology, The Scripps Research Institute, Jupiter, Florida 33458
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Michael Farzan
1Department of Immunology and Microbial Science, The Scripps Research Institute, Jupiter, FL 33458, USA
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  • For correspondence: hchoe@scripps.edu mfarzan@scripps.edu
Hyeryun Choe
1Department of Immunology and Microbial Science, The Scripps Research Institute, Jupiter, FL 33458, USA
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  • For correspondence: hchoe@scripps.edu mfarzan@scripps.edu
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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 SG614 infected 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, SG614 did 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 SG614 is more stable than SD614, consistent with epidemiological data suggesting that viruses with SG614 transmit more efficiently.

Competing Interest Statement

The authors have declared no competing interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted June 12, 2020.
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The D614G mutation in the SARS-CoV-2 spike protein reduces S1 shedding and increases infectivity
Lizhou Zhang, Cody B Jackson, Huihui Mou, Amrita Ojha, Erumbi S Rangarajan, Tina Izard, Michael Farzan, Hyeryun Choe
bioRxiv 2020.06.12.148726; doi: https://doi.org/10.1101/2020.06.12.148726
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The D614G mutation in the SARS-CoV-2 spike protein reduces S1 shedding and increases infectivity
Lizhou Zhang, Cody B Jackson, Huihui Mou, Amrita Ojha, Erumbi S Rangarajan, Tina Izard, Michael Farzan, Hyeryun Choe
bioRxiv 2020.06.12.148726; doi: https://doi.org/10.1101/2020.06.12.148726

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