Distinct conformational states of SARS-CoV-2 spike protein.
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.
Mesh Terms:
Angiotensin-Converting Enzyme 2, Cryoelectron Microscopy, HEK293 Cells, Host-Pathogen Interactions, Humans, Peptidyl-Dipeptidase A, Protein Domains, Protein Multimerization, Protein Structure, Secondary, Receptors, Virus, Spike Glycoprotein, Coronavirus, Virus Internalization
Angiotensin-Converting Enzyme 2, Cryoelectron Microscopy, HEK293 Cells, Host-Pathogen Interactions, Humans, Peptidyl-Dipeptidase A, Protein Domains, Protein Multimerization, Protein Structure, Secondary, Receptors, Virus, Spike Glycoprotein, Coronavirus, Virus Internalization
Science
Date: Sep. 25, 2020
PubMed ID: 32694201
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