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

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 S614G enter ACE2-expressing cells more efficiently than those with S614. 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.

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 Lio, Tina Izard, Christoph Rader, Michael Farzan, Hyeryun Choe