tetano
Editor, Senior Moderator
Science
. 2020 Jul 21;eabd4251.
doi: 10.1126/science.abd4251. Online ahead of print.
Distinct conformational states of SARS-CoV-2 spike protein
Yongfei Cai[SUP] #[/SUP][SUP] 1 2 [/SUP], Jun Zhang[SUP] #[/SUP][SUP] 1 2 [/SUP], Tianshu Xiao[SUP] 1 2 [/SUP], Hanqin Peng[SUP] 1 [/SUP], Sarah M Sterling[SUP] 3 4 [/SUP], Richard M Walsh Jr[SUP] 3 4 [/SUP], Shaun Rawson[SUP] 3 4 5 [/SUP], Sophia Rits-Volloch[SUP] 1 [/SUP], Bing Chen[SUP] 6 2 [/SUP]
Affiliations
Abstract
Intervention strategies are urgently needed to control the SARS-CoV-2 (severe acute respiratory syndrome coronavirus 2) pandemic. The trimeric viral spike (S) protein catalyzes fusion between viral and target cell membranes to initiate infection. Here we report two cryo-EM structures, derived from a preparation of the full-length S protein, representing its prefusion (2.9? resolution) and postfusion (3.0? 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 development of vaccines and therapeutics.
. 2020 Jul 21;eabd4251.
doi: 10.1126/science.abd4251. Online ahead of print.
Distinct conformational states of SARS-CoV-2 spike protein
Yongfei Cai[SUP] #[/SUP][SUP] 1 2 [/SUP], Jun Zhang[SUP] #[/SUP][SUP] 1 2 [/SUP], Tianshu Xiao[SUP] 1 2 [/SUP], Hanqin Peng[SUP] 1 [/SUP], Sarah M Sterling[SUP] 3 4 [/SUP], Richard M Walsh Jr[SUP] 3 4 [/SUP], Shaun Rawson[SUP] 3 4 5 [/SUP], Sophia Rits-Volloch[SUP] 1 [/SUP], Bing Chen[SUP] 6 2 [/SUP]
Affiliations
- PMID: 32694201
- DOI: 10.1126/science.abd4251
Abstract
Intervention strategies are urgently needed to control the SARS-CoV-2 (severe acute respiratory syndrome coronavirus 2) pandemic. The trimeric viral spike (S) protein catalyzes fusion between viral and target cell membranes to initiate infection. Here we report two cryo-EM structures, derived from a preparation of the full-length S protein, representing its prefusion (2.9? resolution) and postfusion (3.0? 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 development of vaccines and therapeutics.