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

Nature Communications
Lizhou ZhangHyeryun Choe


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.


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Methods Mentioned

flow cytometry
surface plasmon resonance

Software Mentioned

CFX Manager
Biacore X100 Evaluation Software
GraphPad Prism
Biacore X100 Control
Image Lab

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