SARS_CoV_2 mutation literature information.


  Structural Impact of Mutation D614G in SARS-CoV-2 Spike Protein: Enhanced Infectivity and Therapeutic Opportunity.
 PMID: 32934770       2020       ACS medicinal chemistry letters
Abstract: Mutation D614G in the spike (S) protein has become dominant, and recent evidence suggests it yields a more stable phenotype with higher transmission efficacy.
Abstract: The D614G substitution creates a sticky packing defect in subunit S1, promoting its association with subunit S2 as a means to stabilize the structure of S1 within the S1/S2 complex.
Introduction: A biophysical/structural analysis of the impact of the D614G


  SARS-CoV-2 infection severity is linked to superior humoral immunity against the spike.
 PMID: 32935099       2020       bioRxiv
Introduction: 5a), suggesting the D614G epitope was not a major antigenic site.
Introduction: SARS-CoV-2 has acquired a D614G mutation within the spike protein and viruses carrying this mutation have since become the dominant circulating strain globally as of early April.
Introduction: These data indicate that the region that encompasses the D614G mutation is not immunodominant or does not affect the antigenicity of epitopes at or near this site.

Browser Board

 Co-occurred Entities




   Filtrator