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Structural impact on SARS-CoV-2 spike protein by D614G substitution.
bioRxiv ; 2020 Oct 20.
Article in English | MEDLINE | ID: covidwho-900758
Preprint
This scientific journal article is probably based on a previously available preprint. It has been identified through a machine matching algorithm, human confirmation is still pending.
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ABSTRACT
Substitution for aspartic acid by glycine at position 614 in the spike (S) protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of the ongoing pandemic, appears to facilitate rapid viral spread. The G614 variant has now replaced the D614-carrying virus as the dominant circulating strain. We report here cryo-EM structures of a full-length S trimer carrying G614, which adopts three distinct prefusion conformations differing primarily by the position of one receptor-binding domain (RBD). 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. The loop transition may also modulate structural rearrangements of S protein required for membrane fusion. These findings extend our understanding of viral entry and suggest an improved immunogen for vaccine development.

Full text: Available Collection: International databases Database: MEDLINE Type of study: Experimental Studies Topics: Vaccines / Variants Language: English Year: 2020 Document Type: Article

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Full text: Available Collection: International databases Database: MEDLINE Type of study: Experimental Studies Topics: Vaccines / Variants Language: English Year: 2020 Document Type: Article