7n1v

From Proteopedia

Jump to: navigation, search

Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants

Structural highlights

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.5Å
Ligands:FUC, MAN, NAG
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

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-EM 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 the accessibility of its receptor binding domain and also 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.

Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants.,Cai Y, Zhang J, Xiao T, Lavine CL, Rawson S, Peng H, Zhu H, Anand K, Tong P, Gautam A, Lu S, Sterling SM, Walsh RM Jr, Rits-Volloch S, Lu J, Wesemann DR, Yang W, Seaman MS, Chen B Science. 2021 Jun 24. pii: science.abi9745. doi: 10.1126/science.abi9745. PMID:34168070[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Loading citation details..
Citations
reviews cite this structure
No citations found

References

  1. Cai Y, Zhang J, Xiao T, Lavine CL, Rawson S, Peng H, Zhu H, Anand K, Tong P, Gautam A, Lu S, Sterling SM, Walsh RM Jr, Rits-Volloch S, Lu J, Wesemann DR, Yang W, Seaman MS, Chen B. Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants. Science. 2021 Jun 24. pii: science.abi9745. doi: 10.1126/science.abi9745. PMID:34168070 doi:http://dx.doi.org/10.1126/science.abi9745

Contents


PDB ID 7n1v

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools