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Structure paper

TitleStructural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants.
Journal, issue, pagesScience, Vol. 373, Issue 6555, Page 642-648, Year 2021
Publish dateAug 6, 2021
AuthorsYongfei Cai / Jun Zhang / Tianshu Xiao / Christy L Lavine / Shaun Rawson / Hanqin Peng / Haisun Zhu / Krishna Anand / Pei Tong / Avneesh Gautam / Shen Lu / Sarah M Sterling / Richard M Walsh / Sophia Rits-Volloch / Jianming Lu / Duane R Wesemann / Wei Yang / Michael S Seaman / Bing Chen /
PubMed AbstractSeveral fast-spreading variants of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have become the dominant circulating strains in the COVID-19 pandemic. We report here cryo-electron ...Several fast-spreading variants of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have become the dominant circulating strains in the COVID-19 pandemic. We report here cryo-electron microscopy structures of the full-length spike (S) trimers of the B.1.1.7 and B.1.351 variants, as well as their biochemical and antigenic properties. Amino acid substitutions in the B.1.1.7 protein increase both the accessibility of its receptor binding domain and the binding affinity for receptor angiotensin-converting enzyme 2 (ACE2). The enhanced receptor engagement may account for the increased transmissibility. The B.1.351 variant has evolved to reshape antigenic surfaces of the major neutralizing sites on the S protein, making it resistant to some potent neutralizing antibodies. These findings provide structural details on how SARS-CoV-2 has evolved to enhance viral fitness and immune evasion.
External linksScience / PubMed:34168070 / PubMed Central
MethodsEM (single particle)
Resolution2.9 - 4.3 Å
Structure data

24121

7n1q

EMDB-24121, PDB-7n1q:
Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants
Method: EM (single particle) / Resolution: 2.9 Å

24122

7n1t

EMDB-24122, PDB-7n1t:
Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants
Method: EM (single particle) / Resolution: 3.11 Å

24123

7n1u

EMDB-24123, PDB-7n1u:
Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants
Method: EM (single particle) / Resolution: 3.14 Å

24124

7n1v

EMDB-24124, PDB-7n1v:
Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants
Method: EM (single particle) / Resolution: 3.21 Å

24125

7n1w

EMDB-24125, PDB-7n1w:
Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants
Method: EM (single particle) / Resolution: 3.33 Å

24126

7n1x

EMDB-24126, PDB-7n1x:
Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants
Method: EM (single particle) / Resolution: 4.0 Å

24127

7n1y

EMDB-24127, PDB-7n1y:
Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants
Method: EM (single particle) / Resolution: 4.3 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • severe acute respiratory syndrome coronavirus 2
KeywordsVIRAL PROTEIN

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