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Structural impact on SARS-CoV-2 spike protein by D614G substitution #MMPMID33727252
Zhang J; Cai Y; Xiao T; Lu J; Peng H; Sterling SM; Walsh RM Jr; Rits-Volloch S; Zhu H; Woosley AN; Yang W; Sliz P; Chen B
Science 2021[Apr]; 372 (6541): 525-530 PMID33727252show ga
Substitution for aspartic acid (D) by glycine (G) at position 614 in the spike (S) protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) appears to facilitate rapid viral spread. The G614 strain and its recent variants are now the dominant circulating forms. Here, we report cryo-electron microscopy structures of a full-length G614 S trimer, which adopts three distinct prefusion conformations that differ primarily by the position of one receptor-binding domain. A loop disordered in the D614 S trimer wedges between domains within a protomer in the G614 spike. This added interaction appears to prevent premature dissociation of the G614 trimer-effectively increasing the number of functional spikes and enhancing infectivity-and to modulate structural rearrangements for membrane fusion. These findings extend our understanding of viral entry and suggest an improved immunogen for vaccine development.
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Science 2021 ; 372 (6541): 525-530
