SrasV1, 2020, Analysis, bibRecord, 000199

Structure of mouse coronavirus spike protein complexed with receptor reveals mechanism for viral entry.

Identifieur interne : 000199 ( 2020/Analysis ); précédent : 000198; suivant : 000200

Structure of mouse coronavirus spike protein complexed with receptor reveals mechanism for viral entry.

Auteurs : Jian Shang [États-Unis] ; Yushun Wan [États-Unis] ; Chang Liu [États-Unis] ; Boyd Yount [États-Unis] ; Kendra Gully [États-Unis] ; Yang Yang [États-Unis] ; Ashley Auerbach [États-Unis] ; Guiqing Peng [République populaire de Chine] ; Ralph Baric [États-Unis] ; Fang Li [États-Unis]

Source :

PLoS pathogens [ 1553-7374 ] ; 2020.

RBID : pubmed:32150576

Descripteurs français

English descriptors

KwdEn :
- Animals, Carcinoembryonic Antigen (chemistry), Carcinoembryonic Antigen (metabolism), Carcinoembryonic Antigen (ultrastructure), Cell Line, Tumor, Cryoelectron Microscopy, HEK293 Cells, Humans, Membrane Fusion, Mice, Models, Molecular, Murine hepatitis virus (chemistry), Murine hepatitis virus (physiology), Protein Binding, Protein Conformation, Protein Conformation, alpha-Helical, Protein Domains, Protein Multimerization, Proteolysis, Receptors, Virus (chemistry), Receptors, Virus (metabolism), Receptors, Virus (ultrastructure), Recombinant Proteins (chemistry), Recombinant Proteins (metabolism), SARS Virus (chemistry), Spike Glycoprotein, Coronavirus (chemistry), Spike Glycoprotein, Coronavirus (metabolism), Spike Glycoprotein, Coronavirus (ultrastructure), Virus Attachment, Virus Internalization.
MESH :
- chemical , chemistry : Carcinoembryonic Antigen, Receptors, Virus, Recombinant Proteins, Spike Glycoprotein, Coronavirus.
- chemical , metabolism : Carcinoembryonic Antigen, Receptors, Virus, Recombinant Proteins, Spike Glycoprotein, Coronavirus.
- chemical , ultrastructure : Carcinoembryonic Antigen, Receptors, Virus, Spike Glycoprotein, Coronavirus.
- chemistry : Murine hepatitis virus, SARS Virus.
- physiology : Murine hepatitis virus.
- Animals, Cell Line, Tumor, Cryoelectron Microscopy, HEK293 Cells, Humans, Membrane Fusion, Mice, Models, Molecular, Protein Binding, Protein Conformation, Protein Conformation, alpha-Helical, Protein Domains, Protein Multimerization, Proteolysis, Virus Attachment, Virus Internalization.

Abstract

Coronaviruses recognize a variety of receptors using different domains of their envelope-anchored spike protein. How these diverse receptor recognition patterns affect viral entry is unknown. Mouse hepatitis coronavirus (MHV) is the only known coronavirus that uses the N-terminal domain (NTD) of its spike to recognize a protein receptor, CEACAM1a. Here we determined the cryo-EM structure of MHV spike complexed with mouse CEACAM1a. The trimeric spike contains three receptor-binding S1 heads sitting on top of a trimeric membrane-fusion S2 stalk. Three receptor molecules bind to the sides of the spike trimer, where three NTDs are located. Receptor binding induces structural changes in the spike, weakening the interactions between S1 and S2. Using protease sensitivity and negative-stain EM analyses, we further showed that after protease treatment of the spike, receptor binding facilitated the dissociation of S1 from S2, allowing S2 to transition from pre-fusion to post-fusion conformation. Together these results reveal a new role of receptor binding in MHV entry: in addition to its well-characterized role in viral attachment to host cells, receptor binding also induces the conformational change of the spike and hence the fusion of viral and host membranes. Our study provides new mechanistic insight into coronavirus entry and highlights the diverse entry mechanisms used by different viruses.

DOI: 10.1371/journal.ppat.1008392
PubMed: 32150576

Affiliations:

Links to Exploration step

pubmed:32150576

Le document en format XML

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<term>Carcinoembryonic Antigen (chemistry)</term>
<term>Carcinoembryonic Antigen (metabolism)</term>
<term>Carcinoembryonic Antigen (ultrastructure)</term>
<term>Cell Line, Tumor</term>
<term>Cryoelectron Microscopy</term>
<term>HEK293 Cells</term>
<term>Humans</term>
<term>Membrane Fusion</term>
<term>Mice</term>
<term>Models, Molecular</term>
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<term>Murine hepatitis virus (physiology)</term>
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<term>Antigène carcinoembryonnaire (ultrastructure)</term>
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<term>Cryomicroscopie électronique</term>
<term>Domaines protéiques</term>
<term>Fusion membranaire</term>
<term>Glycoprotéine de spicule des coronavirus ()</term>
<term>Glycoprotéine de spicule des coronavirus (métabolisme)</term>
<term>Glycoprotéine de spicule des coronavirus (ultrastructure)</term>
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<term>Protéines recombinantes ()</term>
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<term>Récepteurs viraux (métabolisme)</term>
<term>Récepteurs viraux (ultrastructure)</term>
<term>Souris</term>
<term>Structure en hélice alpha</term>
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<term>Virus de l'hépatite murine (physiologie)</term>
<term>Virus du SRAS ()</term>
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<term>Recombinant Proteins</term>
<term>Spike Glycoprotein, Coronavirus</term>
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<term>Spike Glycoprotein, Coronavirus</term>
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<term>Glycoprotéine de spicule des coronavirus</term>
<term>Récepteurs viraux</term>
</keywords>
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<term>Cell Line, Tumor</term>
<term>Cryoelectron Microscopy</term>
<term>HEK293 Cells</term>
<term>Humans</term>
<term>Membrane Fusion</term>
<term>Mice</term>
<term>Models, Molecular</term>
<term>Protein Binding</term>
<term>Protein Conformation</term>
<term>Protein Conformation, alpha-Helical</term>
<term>Protein Domains</term>
<term>Protein Multimerization</term>
<term>Proteolysis</term>
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<term>Antigène carcinoembryonnaire</term>
<term>Attachement viral</term>
<term>Cellules HEK293</term>
<term>Conformation des protéines</term>
<term>Cryomicroscopie électronique</term>
<term>Domaines protéiques</term>
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<term>Glycoprotéine de spicule des coronavirus</term>
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<front><div type="abstract" xml:lang="en">Coronaviruses recognize a variety of receptors using different domains of their envelope-anchored spike protein. How these diverse receptor recognition patterns affect viral entry is unknown. Mouse hepatitis coronavirus (MHV) is the only known coronavirus that uses the N-terminal domain (NTD) of its spike to recognize a protein receptor, CEACAM1a. Here we determined the cryo-EM structure of MHV spike complexed with mouse CEACAM1a. The trimeric spike contains three receptor-binding S1 heads sitting on top of a trimeric membrane-fusion S2 stalk. Three receptor molecules bind to the sides of the spike trimer, where three NTDs are located. Receptor binding induces structural changes in the spike, weakening the interactions between S1 and S2. Using protease sensitivity and negative-stain EM analyses, we further showed that after protease treatment of the spike, receptor binding facilitated the dissociation of S1 from S2, allowing S2 to transition from pre-fusion to post-fusion conformation. Together these results reveal a new role of receptor binding in MHV entry: in addition to its well-characterized role in viral attachment to host cells, receptor binding also induces the conformational change of the spike and hence the fusion of viral and host membranes. Our study provides new mechanistic insight into coronavirus entry and highlights the diverse entry mechanisms used by different viruses.</div>
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<country name="République populaire de Chine"><region name="Hubei"><name sortKey="Peng, Guiqing" sort="Peng, Guiqing" uniqKey="Peng G" first="Guiqing" last="Peng">Guiqing Peng</name>
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</record>

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EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/2020/Analysis

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000199 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/2020/Analysis/biblio.hfd -nk 000199 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Sante
   |area=    SrasV1
   |flux=    2020
   |étape=   Analysis
   |type=    RBID
   |clé=     pubmed:32150576
   |texte=   Structure of mouse coronavirus spike protein complexed with receptor reveals mechanism for viral entry.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/2020/Analysis/RBID.i   -Sk "pubmed:32150576" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/2020/Analysis/biblio.hfd   \
       | NlmPubMed2Wicri -a SrasV1

This area was generated with Dilib version V0.6.33.
Data generation: Tue Apr 28 14:49:16 2020. Site generation: Sat Mar 27 22:06:49 2021

Serveur d'exploration SRAS

Structure of mouse coronavirus spike protein complexed with receptor reveals mechanism for viral entry.

Structure of mouse coronavirus spike protein complexed with receptor reveals mechanism for viral entry.

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Abstract

Links toward previous steps (curation, corpus...)

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Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki

	Serveur d'exploration SRAS
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.