SrasV1, PubMed, Curation, bibRecord, 000B38

Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains.

Identifieur interne : 000B38 ( PubMed/Curation ); précédent : 000B37; suivant : 000B39

Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains.

Source :

Nature communications [ 2041-1723 ] ; 2017.

RBID : pubmed:28393837

Descripteurs français

English descriptors

KwdEn :
- Antibodies, Neutralizing, Antiviral Agents (pharmacology), Cryoelectron Microscopy, Glycoproteins (chemistry), Glycoproteins (ultrastructure), Glycosylation, Membrane Fusion (drug effects), Middle East Respiratory Syndrome Coronavirus (ultrastructure), Models, Molecular, Protein Binding, Protein Domains, Protein Multimerization, Receptors, Virus (metabolism), SARS Virus (ultrastructure), Spike Glycoprotein, Coronavirus (chemistry), Spike Glycoprotein, Coronavirus (ultrastructure).
MESH :
- chemical , chemistry : Glycoproteins, Spike Glycoprotein, Coronavirus.
- chemical , metabolism : Receptors, Virus.
- chemical , pharmacology : Antiviral Agents.
- chemical , ultrastructure : Glycoproteins, Spike Glycoprotein, Coronavirus.
- chemical : Antibodies, Neutralizing.
- drug effects : Membrane Fusion.
- ultrastructure : Middle East Respiratory Syndrome Coronavirus, SARS Virus.
- Cryoelectron Microscopy, Glycosylation, Models, Molecular, Protein Binding, Protein Domains, Protein Multimerization.

Abstract

The envelope spike (S) proteins of MERS-CoV and SARS-CoV determine the virus host tropism and entry into host cells, and constitute a promising target for the development of prophylactics and therapeutics. Here, we present high-resolution structures of the trimeric MERS-CoV and SARS-CoV S proteins in its pre-fusion conformation by single particle cryo-electron microscopy. The overall structures resemble that from other coronaviruses including HKU1, MHV and NL63 reported recently, with the exception of the receptor binding domain (RBD). We captured two states of the RBD with receptor binding region either buried (lying state) or exposed (standing state), demonstrating an inherently flexible RBD readily recognized by the receptor. Further sequence conservation analysis of six human-infecting coronaviruses revealed that the fusion peptide, HR1 region and the central helix are potential targets for eliciting broadly neutralizing antibodies.

DOI: 10.1038/ncomms15092
PubMed: 28393837

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<term>Glycoproteins (ultrastructure)</term>
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<front><div type="abstract" xml:lang="en">The envelope spike (S) proteins of MERS-CoV and SARS-CoV determine the virus host tropism and entry into host cells, and constitute a promising target for the development of prophylactics and therapeutics. Here, we present high-resolution structures of the trimeric MERS-CoV and SARS-CoV S proteins in its pre-fusion conformation by single particle cryo-electron microscopy. The overall structures resemble that from other coronaviruses including HKU1, MHV and NL63 reported recently, with the exception of the receptor binding domain (RBD). We captured two states of the RBD with receptor binding region either buried (lying state) or exposed (standing state), demonstrating an inherently flexible RBD readily recognized by the receptor. Further sequence conservation analysis of six human-infecting coronaviruses revealed that the fusion peptide, HR1 region and the central helix are potential targets for eliciting broadly neutralizing antibodies.</div>
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<Abstract><AbstractText>The envelope spike (S) proteins of MERS-CoV and SARS-CoV determine the virus host tropism and entry into host cells, and constitute a promising target for the development of prophylactics and therapeutics. Here, we present high-resolution structures of the trimeric MERS-CoV and SARS-CoV S proteins in its pre-fusion conformation by single particle cryo-electron microscopy. The overall structures resemble that from other coronaviruses including HKU1, MHV and NL63 reported recently, with the exception of the receptor binding domain (RBD). We captured two states of the RBD with receptor binding region either buried (lying state) or exposed (standing state), demonstrating an inherently flexible RBD readily recognized by the receptor. Further sequence conservation analysis of six human-infecting coronaviruses revealed that the fusion peptide, HR1 region and the central helix are potential targets for eliciting broadly neutralizing antibodies.</AbstractText>
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<AffiliationInfo><Affiliation>CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.</Affiliation>
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<ForeName>Duanfang</ForeName>
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</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Zhang</LastName>
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<AffiliationInfo><Affiliation>Laboratory of Protein Engineering and Vaccines, Tianjin Institute of Biotechnology, Tianjin 300308, China.</Affiliation>
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Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains.

Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains.

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