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Distinct conformational states of SARS-CoV-2 spike protein.
Cai, Yongfei; Zhang, Jun; Xiao, Tianshu; Peng, Hanqin; Sterling, Sarah M; Walsh, Richard M; Rawson, Shaun; Rits-Volloch, Sophia; Chen, Bing.
  • Cai Y; Division of Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA.
  • Zhang J; Department of Pediatrics, Harvard Medical School, Boston, MA 02115, USA.
  • Xiao T; Division of Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA.
  • Peng H; Department of Pediatrics, Harvard Medical School, Boston, MA 02115, USA.
  • Sterling SM; Division of Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA.
  • Walsh RM; Department of Pediatrics, Harvard Medical School, Boston, MA 02115, USA.
  • Rawson S; Division of Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA.
  • Rits-Volloch S; The Harvard Cryo-EM Center for Structural Biology, Harvard Medical School, Boston, MA 02115, USA.
  • Chen B; Department of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115, USA.
Science ; 369(6511): 1586-1592, 2020 09 25.
Article in English | MEDLINE | ID: covidwho-2038226
ABSTRACT
Intervention strategies are urgently needed to control the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic. The trimeric viral spike (S) protein catalyzes fusion between viral and target cell membranes to initiate infection. Here, we report two cryo-electron microscopy structures derived from a preparation of the full-length S protein, representing its prefusion (2.9-angstrom resolution) and postfusion (3.0-angstrom resolution) conformations, respectively. The spontaneous transition to the postfusion state is independent of target cells. The prefusion trimer has three receptor-binding domains clamped down by a segment adjacent to the fusion peptide. The postfusion structure is strategically decorated by N-linked glycans, suggesting possible protective roles against host immune responses and harsh external conditions. These findings advance our understanding of SARS-CoV-2 entry and may guide the development of vaccines and therapeutics.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Host-Pathogen Interactions / Spike Glycoprotein, Coronavirus Topics: Vaccines Limits: Humans Language: English Journal: Science Year: 2020 Document Type: Article Affiliation country: Science.abd4251

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Host-Pathogen Interactions / Spike Glycoprotein, Coronavirus Topics: Vaccines Limits: Humans Language: English Journal: Science Year: 2020 Document Type: Article Affiliation country: Science.abd4251