Lizhou Zhang, Cody B Jackson, H. Mou, Amrita Ojha, Haiyong Peng, Brian D. Quinlan, E. Rangarajan, Andi Pan, A. Vanderheiden, M. Suthar, Wenhui Li, T. Izard, C. Rader, M. Farzan, H. Choe
Nature communications, 2020
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.
Cited by 200 publications.
Field of study: Biology