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Structure paper

TitleA thermostable, closed SARS-CoV-2 spike protein trimer.
Journal, issue, pagesNat Struct Mol Biol, Vol. 27, Issue 10, Page 934-941, Year 2020
Publish dateJul 31, 2020
AuthorsXiaoli Xiong / Kun Qu / Katarzyna A Ciazynska / Myra Hosmillo / Andrew P Carter / Soraya Ebrahimi / Zunlong Ke / Sjors H W Scheres / Laura Bergamaschi / Guinevere L Grice / Ying Zhang / / James A Nathan / Stephen Baker / Leo C James / Helen E Baxendale / Ian Goodfellow / Rainer Doffinger / John A G Briggs /
PubMed AbstractThe spike (S) protein of SARS-CoV-2 mediates receptor binding and cell entry and is the dominant target of the immune system. It exhibits substantial conformational flexibility. It transitions from ...The spike (S) protein of SARS-CoV-2 mediates receptor binding and cell entry and is the dominant target of the immune system. It exhibits substantial conformational flexibility. It transitions from closed to open conformations to expose its receptor-binding site and, subsequently, from prefusion to postfusion conformations to mediate fusion of viral and cellular membranes. S-protein derivatives are components of vaccine candidates and diagnostic assays, as well as tools for research into the biology and immunology of SARS-CoV-2. Here we have designed mutations in S that allow the production of thermostable, disulfide-bonded S-protein trimers that are trapped in the closed, prefusion state. Structures of the disulfide-stabilized and non-disulfide-stabilized proteins reveal distinct closed and locked conformations of the S trimer. We demonstrate that the designed, thermostable, closed S trimer can be used in serological assays. This protein has potential applications as a reagent for serology, virology and as an immunogen.
External linksNat Struct Mol Biol / PubMed:32737467 / PubMed Central
MethodsEM (single particle)
Resolution3.0 - 3.5 Å
Structure data

11329

6zox

EMDB-11329, PDB-6zox:
Structure of Disulphide-stabilized SARS-CoV-2 Spike Protein Trimer (x2 disulphide-bond mutant, G413C, V987C, single Arg S1/S2 cleavage site)
Method: EM (single particle) / Resolution: 3.0 Å

11330

6zoy

EMDB-11330, PDB-6zoy:
Structure of Disulphide-stabilized SARS-CoV-2 Spike Protein Trimer (x1 disulphide-bond mutant, S383C, D985C, K986P, V987P, single Arg S1/S2 cleavage site) in Closed State
Method: EM (single particle) / Resolution: 3.1 Å

11331

6zoz

EMDB-11331, PDB-6zoz:
Structure of Disulphide-stabilized SARS-CoV-2 Spike Protein Trimer (x1 disulphide-bond mutant, S383C, D985C, K986P, V987P, single Arg S1/S2 cleavage site) in Locked State
Method: EM (single particle) / Resolution: 3.5 Å

11332

6zp0

EMDB-11332, PDB-6zp0:
Structure of SARS-CoV-2 Spike Protein Trimer (single Arg S1/S2 cleavage site) in Closed State
Method: EM (single particle) / Resolution: 3.0 Å

11333

6zp1

EMDB-11333, PDB-6zp1:
Structure of SARS-CoV-2 Spike Protein Trimer (K986P, V987P, single Arg S1/S2 cleavage site) in Closed State
Method: EM (single particle) / Resolution: 3.3 Å

11334

6zp2

EMDB-11334, PDB-6zp2:
Structure of SARS-CoV-2 Spike Protein Trimer (K986P, V987P, single Arg S1/S2 cleavage site) in Locked State
Method: EM (single particle) / Resolution: 3.1 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-BLA:
BILIVERDINE IX ALPHA

ChemComp-EIC:
LINOLEIC ACID / Linoleic acid

Source
  • severe acute respiratory syndrome coronavirus 2
KeywordsVIRAL PROTEIN / coronavirus / SARS-CoV-2 / Spike protein / S protein / S antigen / COVID-19 / receptor binding / membrane fusion / vaccine design

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