MersV1, PubMed, Curation, bibRecord, 001227

Pre-fusion structure of a human coronavirus spike protein.

Identifieur interne : 001227 ( PubMed/Curation ); précédent : 001226; suivant : 001228

Pre-fusion structure of a human coronavirus spike protein.

Auteurs : Robert N. Kirchdoerfer [États-Unis] ; Christopher A. Cottrell [États-Unis] ; Nianshuang Wang [États-Unis] ; Jesper Pallesen [États-Unis] ; Hadi M. Yassine [États-Unis] ; Hannah L. Turner [États-Unis] ; Kizzmekia S. Corbett [États-Unis] ; Barney S. Graham [États-Unis] ; Jason S. Mclellan [États-Unis] ; Andrew B. Ward [États-Unis]

Source :

Nature [ 1476-4687 ] ; 2016.

RBID : pubmed:26935699

Descripteurs français

English descriptors

KwdEn :
- Cell Line, Coronavirus (chemistry), Coronavirus (ultrastructure), Cryoelectron Microscopy, Humans, Membrane Fusion, Models, Molecular, Protein Binding, Protein Multimerization, Protein Structure, Quaternary, Protein Structure, Tertiary, Protein Subunits (chemistry), Protein Subunits (metabolism), Proteolysis, Receptors, Virus (metabolism), Spike Glycoprotein, Coronavirus (chemistry), Spike Glycoprotein, Coronavirus (metabolism), Spike Glycoprotein, Coronavirus (ultrastructure), Viral Vaccines (chemistry), Viral Vaccines (immunology), Virus Internalization.
MESH :
- chemical , chemistry : Protein Subunits, Spike Glycoprotein, Coronavirus, Viral Vaccines.
- chemistry : Coronavirus.
- chemical , immunology : Viral Vaccines.
- chemical , metabolism : Protein Subunits, Receptors, Virus, Spike Glycoprotein, Coronavirus.
- ultrastructure : Coronavirus, Spike Glycoprotein, Coronavirus.
- Cell Line, Cryoelectron Microscopy, Humans, Membrane Fusion, Models, Molecular, Protein Binding, Protein Multimerization, Protein Structure, Quaternary, Protein Structure, Tertiary, Proteolysis, Virus Internalization.

Abstract

HKU1 is a human betacoronavirus that causes mild yet prevalent respiratory disease, and is related to the zoonotic SARS and MERS betacoronaviruses, which have high fatality rates and pandemic potential. Cell tropism and host range is determined in part by the coronavirus spike (S) protein, which binds cellular receptors and mediates membrane fusion. As the largest known class I fusion protein, its size and extensive glycosylation have hindered structural studies of the full ectodomain, thus preventing a molecular understanding of its function and limiting development of effective interventions. Here we present the 4.0 Å resolution structure of the trimeric HKU1 S protein determined using single-particle cryo-electron microscopy. In the pre-fusion conformation, the receptor-binding subunits, S1, rest above the fusion-mediating subunits, S2, preventing their conformational rearrangement. Surprisingly, the S1 C-terminal domains are interdigitated and form extensive quaternary interactions that occlude surfaces known in other coronaviruses to bind protein receptors. These features, along with the location of the two protease sites known to be important for coronavirus entry, provide a structural basis to support a model of membrane fusion mediated by progressive S protein destabilization through receptor binding and proteolytic cleavage. These studies should also serve as a foundation for the structure-based design of betacoronavirus vaccine immunogens.

DOI: 10.1038/nature17200
PubMed: 26935699

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<front><div type="abstract" xml:lang="en">HKU1 is a human betacoronavirus that causes mild yet prevalent respiratory disease, and is related to the zoonotic SARS and MERS betacoronaviruses, which have high fatality rates and pandemic potential. Cell tropism and host range is determined in part by the coronavirus spike (S) protein, which binds cellular receptors and mediates membrane fusion. As the largest known class I fusion protein, its size and extensive glycosylation have hindered structural studies of the full ectodomain, thus preventing a molecular understanding of its function and limiting development of effective interventions. Here we present the 4.0 Å resolution structure of the trimeric HKU1 S protein determined using single-particle cryo-electron microscopy. In the pre-fusion conformation, the receptor-binding subunits, S1, rest above the fusion-mediating subunits, S2, preventing their conformational rearrangement. Surprisingly, the S1 C-terminal domains are interdigitated and form extensive quaternary interactions that occlude surfaces known in other coronaviruses to bind protein receptors. These features, along with the location of the two protease sites known to be important for coronavirus entry, provide a structural basis to support a model of membrane fusion mediated by progressive S protein destabilization through receptor binding and proteolytic cleavage. These studies should also serve as a foundation for the structure-based design of betacoronavirus vaccine immunogens. </div>
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<Abstract><AbstractText>HKU1 is a human betacoronavirus that causes mild yet prevalent respiratory disease, and is related to the zoonotic SARS and MERS betacoronaviruses, which have high fatality rates and pandemic potential. Cell tropism and host range is determined in part by the coronavirus spike (S) protein, which binds cellular receptors and mediates membrane fusion. As the largest known class I fusion protein, its size and extensive glycosylation have hindered structural studies of the full ectodomain, thus preventing a molecular understanding of its function and limiting development of effective interventions. Here we present the 4.0 Å resolution structure of the trimeric HKU1 S protein determined using single-particle cryo-electron microscopy. In the pre-fusion conformation, the receptor-binding subunits, S1, rest above the fusion-mediating subunits, S2, preventing their conformational rearrangement. Surprisingly, the S1 C-terminal domains are interdigitated and form extensive quaternary interactions that occlude surfaces known in other coronaviruses to bind protein receptors. These features, along with the location of the two protease sites known to be important for coronavirus entry, provide a structural basis to support a model of membrane fusion mediated by progressive S protein destabilization through receptor binding and proteolytic cleavage. These studies should also serve as a foundation for the structure-based design of betacoronavirus vaccine immunogens. </AbstractText>
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Pre-fusion structure of a human coronavirus spike protein.

Pre-fusion structure of a human coronavirus spike protein.

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