Статья

Distinct conformational states of SARS-CoV-2 spike protein

Yongfei CaiDepartment of Pediatrics, Harvard Medical School, Boston, MA 02115, USAJun ZhangDepartment of Pediatrics, Harvard Medical School, Boston, MA 02115, USATianshu XiaoDepartment of Pediatrics, Harvard Medical School, Boston, MA 02115, USAHanqin PengDivision of Molecular Medicine, Boston Children’s Hospital, Boston, MA 02115, USASarah M. SterlingDepartment of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115, USARichard M. WalshDepartment of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115, USAShaun RawsonDepartment of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115, USASophia Rits‐VollochDivision of Molecular Medicine, Boston Children’s Hospital, Boston, MA 02115, USABing ChenDepartment of Pediatrics, Harvard Medical School, Boston, MA 02115, USA

2020en

ABI

Аннотация

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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Идентификаторы

DOI: 10.1126/science.abd4251

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