SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity

Lizhou Zhang, Cody B. Jackson, Huihui Mou, Amrita Ojha, Haiyong Peng, Brian D. Quinlan, Erumbi S. Rangarajan, Andi Pan, Abigail Vanderheiden, Mehul S. Suthar, Wenhui Li, Tina Izard, Christoph Rader, Michael Farzan () and Hyeryun Choe ()
Additional contact information
Lizhou Zhang: The Scripps Research Institute
Cody B. Jackson: The Scripps Research Institute
Huihui Mou: The Scripps Research Institute
Amrita Ojha: The Scripps Research Institute
Haiyong Peng: The Scripps Research Institute
Brian D. Quinlan: The Scripps Research Institute
Erumbi S. Rangarajan: The Scripps Research Institute
Andi Pan: The Scripps Research Institute
Abigail Vanderheiden: Division of Infectious Disease, Emory University School of Medicine
Mehul S. Suthar: Division of Infectious Disease, Emory University School of Medicine
Wenhui Li: Tsinghua Institute of Multidisciplinary Biomedical Research, Tsinghua University
Tina Izard: The Scripps Research Institute
Christoph Rader: The Scripps Research Institute
Michael Farzan: The Scripps Research Institute
Hyeryun Choe: The Scripps Research Institute

Nature Communications, 2020, vol. 11, issue 1, 1-9

Abstract: Abstract SARS-CoV-2 variants with spike (S)-protein D614G mutations now predominate globally. We therefore compare the properties of the mutated S protein (SG614) with the original (SD614). We report here pseudoviruses carrying SG614 enter ACE2-expressing cells more efficiently than those with SD614. This increased entry correlates with less S1-domain shedding and higher S-protein incorporation into the virion. Similar results are obtained with virus-like particles produced with SARS-CoV-2 M, N, E, and S proteins. However, D614G does not alter S-protein binding to ACE2 or neutralization sensitivity of pseudoviruses. Thus, D614G may increase infectivity by assembling more functional S protein into the virion.

Date: 2020
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DOI: 10.1038/s41467-020-19808-4

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