tetano
Editor, Senior Moderator
Nature
. 2020 Aug 17.
doi: 10.1038/s41586-020-2665-2. Online ahead of print.
Structures and distributions of SARS-CoV-2 spike proteins on intact virions
Zunlong Ke[SUP] 1 [/SUP], Joaquin Oton[SUP] 1 [/SUP], Kun Qu[SUP] 1 [/SUP], Mirko Cortese[SUP] 2 [/SUP], Vojtech Zila[SUP] 3 [/SUP], Lesley McKeane[SUP] 4 [/SUP], Takanori Nakane[SUP] 1 [/SUP], Jasenko Zivanov[SUP] 1 [/SUP], Christopher J Neufeldt[SUP] 2 [/SUP], Berati Cerikan[SUP] 2 [/SUP], John M Lu[SUP] 1 [/SUP], Julia Peukes[SUP] 1 [/SUP], Xiaoli Xiong[SUP] 1 [/SUP], Hans-Georg Kr?usslich[SUP] 3 5 [/SUP], Sjors H W Scheres[SUP] 1 [/SUP], Ralf Bartenschlager[SUP] 2 5 [/SUP], John A G Briggs[SUP] 6 [/SUP]
Affiliations
Abstract
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude[SUP]1[/SUP]. Heavily glycosylated S trimers bind the ACE2 receptor and mediate entry of virions into target cells[SUP]2-6[/SUP]. S exhibits extensive conformational flexibility: it modulates exposure of its receptor binding site and later undergoes complete structural rearrangement to drive fusion of viral and cellular membranes[SUP]2,7,8[/SUP]. The structures and conformations of soluble, overexpressed, purified S proteins have been studied in detail using cryo-electron microscopy[SUP]2,7,9-12[/SUP]. The structure and distribution of S on the virion surface, however, has not been characterized. Here we applied cryo-electron microscopy and tomography to image intact SARS-CoV-2 virions, determining the high-resolution structure, conformational flexibility and distribution of S trimers in situ on the virion surface. These results reveal the conformations of S present on the virion, and provide a basis from which to understand interactions between S and neutralizing antibodies during infection or vaccination.
. 2020 Aug 17.
doi: 10.1038/s41586-020-2665-2. Online ahead of print.
Structures and distributions of SARS-CoV-2 spike proteins on intact virions
Zunlong Ke[SUP] 1 [/SUP], Joaquin Oton[SUP] 1 [/SUP], Kun Qu[SUP] 1 [/SUP], Mirko Cortese[SUP] 2 [/SUP], Vojtech Zila[SUP] 3 [/SUP], Lesley McKeane[SUP] 4 [/SUP], Takanori Nakane[SUP] 1 [/SUP], Jasenko Zivanov[SUP] 1 [/SUP], Christopher J Neufeldt[SUP] 2 [/SUP], Berati Cerikan[SUP] 2 [/SUP], John M Lu[SUP] 1 [/SUP], Julia Peukes[SUP] 1 [/SUP], Xiaoli Xiong[SUP] 1 [/SUP], Hans-Georg Kr?usslich[SUP] 3 5 [/SUP], Sjors H W Scheres[SUP] 1 [/SUP], Ralf Bartenschlager[SUP] 2 5 [/SUP], John A G Briggs[SUP] 6 [/SUP]
Affiliations
- PMID: 32805734
- DOI: 10.1038/s41586-020-2665-2
Abstract
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude[SUP]1[/SUP]. Heavily glycosylated S trimers bind the ACE2 receptor and mediate entry of virions into target cells[SUP]2-6[/SUP]. S exhibits extensive conformational flexibility: it modulates exposure of its receptor binding site and later undergoes complete structural rearrangement to drive fusion of viral and cellular membranes[SUP]2,7,8[/SUP]. The structures and conformations of soluble, overexpressed, purified S proteins have been studied in detail using cryo-electron microscopy[SUP]2,7,9-12[/SUP]. The structure and distribution of S on the virion surface, however, has not been characterized. Here we applied cryo-electron microscopy and tomography to image intact SARS-CoV-2 virions, determining the high-resolution structure, conformational flexibility and distribution of S trimers in situ on the virion surface. These results reveal the conformations of S present on the virion, and provide a basis from which to understand interactions between S and neutralizing antibodies during infection or vaccination.