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The SARS-CoV-2 spike reversibly samples an open-trimer conformation exposing novel epitopes.
Costello, Shawn M; Shoemaker, Sophie R; Hobbs, Helen T; Nguyen, Annalee W; Hsieh, Ching-Lin; Maynard, Jennifer A; McLellan, Jason S; Pak, John E; Marqusee, Susan.
Afiliação
  • Costello SM; Biophysics Graduate Program, University of California, Berkeley, CA, USA.
  • Shoemaker SR; Department of Molecular and Cell Biology, University of California, Berkeley, CA, USA.
  • Hobbs HT; Department of Chemistry, University of California, Berkeley, CA, USA.
  • Nguyen AW; Department of Chemical Engineering, The University of Texas at Austin, Austin, TX, USA.
  • Hsieh CL; Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX, USA.
  • Maynard JA; Department of Chemical Engineering, The University of Texas at Austin, Austin, TX, USA.
  • McLellan JS; Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX, USA.
  • Pak JE; Chan Zuckerberg Biohub, San Francisco, CA, USA.
  • Marqusee S; Department of Molecular and Cell Biology, University of California, Berkeley, CA, USA. marqusee@berkeley.edu.
Nat Struct Mol Biol ; 29(3): 229-238, 2022 03.
Article em En | MEDLINE | ID: mdl-35236990
ABSTRACT
Current COVID-19 vaccines and many clinical diagnostics are based on the structure and function of the SARS-CoV-2 spike ectodomain. Using hydrogen-deuterium exchange monitored by mass spectrometry, we have uncovered that, in addition to the prefusion structure determined by cryo-electron microscopy, this protein adopts an alternative conformation that interconverts slowly with the canonical prefusion structure. This new conformation-an open trimer-contains easily accessible receptor-binding domains. It exposes the conserved trimer interface buried in the prefusion conformation, thus exposing potential epitopes for pan-coronavirus antibody and ligand recognition. The population of this state and kinetics of interconversion are modulated by temperature, receptor binding, antibody binding, and sequence variants observed in the natural population. Knowledge of the structure and populations of this conformation will help improve existing diagnostics, therapeutics, and vaccines.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Glicoproteína da Espícula de Coronavírus / COVID-19 Limite: Humans Idioma: En Revista: Nat Struct Mol Biol Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2022 Tipo de documento: Article País de afiliação: Estados Unidos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Glicoproteína da Espícula de Coronavírus / COVID-19 Limite: Humans Idioma: En Revista: Nat Struct Mol Biol Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2022 Tipo de documento: Article País de afiliação: Estados Unidos