SARS-CoV-2 variants with spike (S)-protein D614G mutations now predominate globally. We therefore compare the properties of the mutated S protein (S G614 ) with the original (S D614 ). We report here pseudoviruses carrying S G614 enter ACE2-expressing cells more efficiently than those with S D614 . 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. SARS-CoV-2 variants with spike (S)-protein D614G mutations currently predominate globally. Here, Zhang et al. hypothesize that D614G variant may increase infectivity by increasing S protein abundance on the virion since pseudoviruses carrying S-G614 incorporate higher amounts of S protein and enter cells more efficiently than those carrying S-D614.
【저자키워드】 SARS-CoV-2, Virology, 【초록키워드】 ACE2, S protein, neutralization, SARS-CoV-2 variant, sensitivity, D614G mutation, SARS-CoV-2 variants, pseudovirus, D614G variant, D614G, virus-like particles, binding, S-protein, pseudoviruses, Virus-like particle, S proteins, virion, ACE2-expressing cells, Alter, Cell, produced, functional, less, mutated, ACE2-expressing cell, 【제목키워드】 D614G mutation, spike-protein, increase,