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Cryo-EM structures of SARS-CoV-2 Omicron BA.2 spike.
Stalls, Victoria; Lindenberger, Jared; Gobeil, Sophie M-C; Henderson, Rory; Parks, Rob; Barr, Maggie; Deyton, Margaret; Martin, Mitchell; Janowska, Katarzyna; Huang, Xiao; May, Aaron; Speakman, Micah; Beaudoin, Esther; Kraft, Bryan; Lu, Xiaozhi; Edwards, Robert J; Eaton, Amanda; Montefiori, David C; Williams, Wilton B; Saunders, Kevin O; Wiehe, Kevin; Haynes, Barton F; Acharya, Priyamvada.
Afiliação
  • Stalls V; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Lindenberger J; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Gobeil SM; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Henderson R; Duke Human Vaccine Institute, Durham, NC 27710, USA; Department of Medicine, Duke University, Durham, NC 27710, USA.
  • Parks R; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Barr M; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Deyton M; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Martin M; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Janowska K; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Huang X; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • May A; Duke Human Vaccine Institute, Durham, NC 27710, USA; Department of Biochemistry, Duke University, Durham, NC 27710, USA.
  • Speakman M; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Beaudoin E; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Kraft B; Department of Medicine, Duke University, Durham, NC 27710, USA.
  • Lu X; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Edwards RJ; Duke Human Vaccine Institute, Durham, NC 27710, USA; Department of Medicine, Duke University, Durham, NC 27710, USA.
  • Eaton A; Duke Human Vaccine Institute, Durham, NC 27710, USA.
  • Montefiori DC; Duke Human Vaccine Institute, Durham, NC 27710, USA; Department of Surgery, Duke University, Durham, NC 27710, USA.
  • Williams WB; Duke Human Vaccine Institute, Durham, NC 27710, USA; Department of Biochemistry, Duke University, Durham, NC 27710, USA.
  • Saunders KO; Duke Human Vaccine Institute, Durham, NC 27710, USA; Department of Surgery, Duke University, Durham, NC 27710, USA.
  • Wiehe K; Duke Human Vaccine Institute, Durham, NC 27710, USA; Department of Medicine, Duke University, Durham, NC 27710, USA.
  • Haynes BF; Duke Human Vaccine Institute, Durham, NC 27710, USA; Department of Medicine, Duke University, Durham, NC 27710, USA; Department of Immunology, Duke University, Durham, NC 27710, USA. Electronic address: barton.haynes@duke.edu.
  • Acharya P; Duke Human Vaccine Institute, Durham, NC 27710, USA; Department of Biochemistry, Duke University, Durham, NC 27710, USA; Department of Surgery, Duke University, Durham, NC 27710, USA. Electronic address: priyamvada.acharya@duke.edu.
Cell Rep ; 39(13): 111009, 2022 06 28.
Article em En | MEDLINE | ID: mdl-35732171
The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron BA.2 sub-lineage has gained in proportion relative to BA.1. Because spike (S) protein variations may underlie differences in their pathobiology, here we determine cryoelectron microscopy (cryo-EM) structures of the BA.2 S ectodomain and compare these with previously determined BA.1 S structures. BA.2 receptor-binding domain (RBD) mutations induce remodeling of the RBD structure, resulting in tighter packing and improved thermostability. Interprotomer RBD interactions are enhanced in the closed (or 3-RBD-down) BA.2 S, while the fusion peptide is less accessible to antibodies than in BA.1. Binding and pseudovirus neutralization assays reveal extensive immune evasion while defining epitopes of two outer RBD face-binding antibodies, DH1044 and DH1193, that neutralize both BA.1 and BA.2. Taken together, our results indicate that stabilization of the closed state through interprotomer RBD-RBD packing is a hallmark of the Omicron variant and show differences in key functional regions in the BA.1 and BA.2 S proteins.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: SARS-CoV-2 / COVID-19 Limite: Humans Idioma: En Ano de publicação: 2022 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: SARS-CoV-2 / COVID-19 Limite: Humans Idioma: En Ano de publicação: 2022 Tipo de documento: Article