• Nature communications · Nov 2020

    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.
    • Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL, USA.
    • Nat Commun. 2020 Nov 26; 11 (1): 6013.

    AbstractSARS-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.

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