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Title | Structural impact on SARS-CoV-2 spike protein by D614G substitution. |
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Journal, issue, pages | Science, Vol. 372, Issue 6541, Page 525-530, Year 2021 |
Publish date | Apr 30, 2021 |
Authors | Jun Zhang / Yongfei Cai / Tianshu Xiao / Jianming Lu / Hanqin Peng / Sarah M Sterling / Richard M Walsh / Sophia Rits-Volloch / Haisun Zhu / Alec N Woosley / Wei Yang / Piotr Sliz / Bing Chen / |
PubMed Abstract | 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. ...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. |
External links | Science / PubMed:33727252 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.2 - 3.5 Å |
Structure data | EMDB-23010, PDB-7krq: EMDB-23011, PDB-7krr: EMDB-23012, PDB-7krs: |
Chemicals | ChemComp-NAG: |
Source |
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Keywords | VIRAL PROTEIN |