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Title: SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity
Abstract 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.
Authors:
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Award ID(s):
2033939
Publication Date:
NSF-PAR ID:
10286963
Journal Name:
Nature Communications
Volume:
11
Issue:
1
ISSN:
2041-1723
Sponsoring Org:
National Science Foundation
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