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Zhang, Lizhou; Jackson, Cody B; Mou, Huihui; Ojha, Amrita; Peng, Haiyong; Quinlan, Brian D; Rangarajan, Erumbi S; Pan, Andi; Vanderheiden, Abigail; Suthar, Mehul S; Li, Wenhui; Izard, Tina; Rader, Christoph; Farzan, Michael; Choe, Hyeryun
Nature communications, 11/2020, Letnik: 11, Številka: 1Journal Article
SARS-CoV-2 variants with spike (S)-protein D614G mutations now predominate globally. We therefore compare the properties of the mutated S protein (S ) with the original (S ). We report here pseudoviruses carrying S enter ACE2-expressing cells more efficiently than those with S . 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.
