Distinct conformational states of SARS-CoV-2 spike protein.
Yongfei CaiJun ZhangTianshu XiaoHanqin PengSarah M SterlingRichard M WalshShaun RawsonSophia Rits-VollochBing ChenPublished in: Science (New York, N.Y.) (2020)
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.
Keyphrases
- sars cov
- respiratory syndrome coronavirus
- electron microscopy
- binding protein
- immune response
- single molecule
- protein protein
- randomized controlled trial
- high resolution
- induced apoptosis
- small molecule
- coronavirus disease
- stem cells
- molecular dynamics
- cell proliferation
- cell therapy
- cell death
- cell cycle arrest
- endoplasmic reticulum stress
- reduced graphene oxide
- inflammatory response
- highly efficient
- bone marrow
- cell surface