Structural basis for coronavirus-mediated membrane fusion. Crystal structure of mouse hepatitis virus spike protein fusion core.
Identifieur interne : 005058 ( Main/Exploration ); précédent : 005057; suivant : 005059Structural basis for coronavirus-mediated membrane fusion. Crystal structure of mouse hepatitis virus spike protein fusion core.
Auteurs : Yanhui Xu [République populaire de Chine] ; Yiwei Liu ; Zhiyong Lou ; Lan Qin ; Xu Li ; Zhihong Bai ; Hai Pang ; Po Tien ; George F. Gao ; Zihe RaoSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2004.
Descripteurs français
- KwdFr :
- Animaux, Concentration en ions d'hydrogène, Conformation des protéines, Coronavirus (métabolisme), Cristallographie aux rayons X, Dimérisation, Données de séquences moléculaires, Escherichia coli (métabolisme), Fusion membranaire, Glycoprotéine de spicule des coronavirus, Glycoprotéine hémagglutinine du virus influenza (métabolisme), Glycoprotéines membranaires (), Glycoprotéines membranaires (métabolisme), Liaison aux protéines, Modèles biologiques, Modèles moléculaires, Motifs d'acides aminés, Peptides (), Protéines de fusion virale (), Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (métabolisme), Similitude de séquences d'acides aminés, Souris, Structure secondaire des protéines, Séquence d'acides aminés, Virus de l'hépatite murine (métabolisme).
- MESH :
- métabolisme : Coronavirus, Escherichia coli, Glycoprotéine hémagglutinine du virus influenza, Glycoprotéines membranaires, Protéines de l'enveloppe virale, Virus de l'hépatite murine.
- Animaux, Concentration en ions d'hydrogène, Conformation des protéines, Cristallographie aux rayons X, Dimérisation, Données de séquences moléculaires, Fusion membranaire, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Liaison aux protéines, Modèles biologiques, Modèles moléculaires, Motifs d'acides aminés, Peptides, Protéines de fusion virale, Protéines de l'enveloppe virale, Similitude de séquences d'acides aminés, Souris, Structure secondaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Motifs, Amino Acid Sequence, Animals, Coronavirus (metabolism), Crystallography, X-Ray, Dimerization, Escherichia coli (metabolism), Hemagglutinin Glycoproteins, Influenza Virus (metabolism), Hydrogen-Ion Concentration, Membrane Fusion, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (metabolism), Mice, Models, Biological, Models, Molecular, Molecular Sequence Data, Murine hepatitis virus (metabolism), Peptides (chemistry), Protein Binding, Protein Conformation, Protein Structure, Secondary, Sequence Homology, Amino Acid, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (metabolism), Viral Fusion Proteins (chemistry).
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Peptides, Viral Envelope Proteins, Viral Fusion Proteins.
- chemical , metabolism : Hemagglutinin Glycoproteins, Influenza Virus, Membrane Glycoproteins, Viral Envelope Proteins.
- metabolism : Coronavirus, Escherichia coli, Murine hepatitis virus.
- Amino Acid Motifs, Amino Acid Sequence, Animals, Crystallography, X-Ray, Dimerization, Hydrogen-Ion Concentration, Membrane Fusion, Mice, Models, Biological, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Conformation, Protein Structure, Secondary, Sequence Homology, Amino Acid, Spike Glycoprotein, Coronavirus.
Abstract
The surface transmembrane glycoprotein is responsible for mediating virion attachment to cell and subsequent virus-cell membrane fusion. However, the molecular mechanisms for the viral entry of coronaviruses remain poorly understood. The crystal structure of the fusion core of mouse hepatitis virus S protein, which represents the first fusion core structure of any coronavirus, reveals a central hydrophobic coiled coil trimer surrounded by three helices in an oblique, antiparallel manner. This structure shares significant similarity with both the low pH-induced conformation of influenza hemagglutinin and fusion core of HIV gp41, indicating that the structure represents a fusion-active state formed after several conformational changes. Our results also indicate that the mechanisms for the viral fusion of coronaviruses are similar to those of influenza virus and HIV. The coiled coil structure has unique features, which are different from other viral fusion cores. Highly conserved heptad repeat 1 (HR1) and HR2 regions in coronavirus spike proteins indicate a similar three-dimensional structure among these fusion cores and common mechanisms for the viral fusion. We have proposed the binding regions of HR1 and HR2 of other coronaviruses and a structure model of their fusion core based on our mouse hepatitis virus fusion core structure and sequence alignment. Drug discovery strategies aimed at inhibiting viral entry by blocking hairpin formation may be applied to the inhibition of a number of emerging infectious diseases, including severe acute respiratory syndrome.
DOI: 10.1074/jbc.M403760200
PubMed: 15123674
Affiliations:
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Crystal structure of mouse hepatitis virus spike protein fusion core.</title><author><name sortKey="Xu, Yanhui" sort="Xu, Yanhui" uniqKey="Xu Y" first="Yanhui" last="Xu">Yanhui Xu</name><affiliation wicri:level="1"><nlm:affiliation>Laboratory of Structural Biology, Tsinghua University, Beijing 100084, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Laboratory of Structural Biology, Tsinghua University, Beijing 100084</wicri:regionArea><placeName><settlement type="city">Pékin</settlement></placeName></affiliation></author><author><name sortKey="Liu, Yiwei" sort="Liu, Yiwei" uniqKey="Liu Y" first="Yiwei" last="Liu">Yiwei Liu</name></author><author><name sortKey="Lou, Zhiyong" sort="Lou, Zhiyong" uniqKey="Lou Z" first="Zhiyong" last="Lou">Zhiyong Lou</name></author><author><name sortKey="Qin, Lan" sort="Qin, Lan" uniqKey="Qin L" first="Lan" last="Qin">Lan Qin</name></author><author><name sortKey="Li, Xu" sort="Li, Xu" uniqKey="Li X" first="Xu" last="Li">Xu Li</name></author><author><name sortKey="Bai, Zhihong" sort="Bai, Zhihong" uniqKey="Bai Z" first="Zhihong" last="Bai">Zhihong Bai</name></author><author><name sortKey="Pang, Hai" sort="Pang, Hai" uniqKey="Pang H" first="Hai" last="Pang">Hai Pang</name></author><author><name sortKey="Tien, Po" sort="Tien, Po" uniqKey="Tien P" first="Po" last="Tien">Po Tien</name></author><author><name sortKey="Gao, George F" sort="Gao, George F" uniqKey="Gao G" first="George F" last="Gao">George F. Gao</name></author><author><name sortKey="Rao, Zihe" sort="Rao, Zihe" uniqKey="Rao Z" first="Zihe" last="Rao">Zihe Rao</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Motifs</term><term>Amino Acid Sequence</term><term>Animals</term><term>Coronavirus (metabolism)</term><term>Crystallography, X-Ray</term><term>Dimerization</term><term>Escherichia coli (metabolism)</term><term>Hemagglutinin Glycoproteins, Influenza Virus (metabolism)</term><term>Hydrogen-Ion Concentration</term><term>Membrane Fusion</term><term>Membrane Glycoproteins (chemistry)</term><term>Membrane Glycoproteins (metabolism)</term><term>Mice</term><term>Models, Biological</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Murine hepatitis virus (metabolism)</term><term>Peptides (chemistry)</term><term>Protein Binding</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term><term>Sequence Homology, Amino Acid</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (metabolism)</term><term>Viral Fusion Proteins (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Concentration en ions d'hydrogène</term><term>Conformation des protéines</term><term>Coronavirus (métabolisme)</term><term>Cristallographie aux rayons X</term><term>Dimérisation</term><term>Données de séquences moléculaires</term><term>Escherichia coli (métabolisme)</term><term>Fusion membranaire</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéine hémagglutinine du virus influenza (métabolisme)</term><term>Glycoprotéines membranaires ()</term><term>Glycoprotéines membranaires (métabolisme)</term><term>Liaison aux protéines</term><term>Modèles biologiques</term><term>Modèles moléculaires</term><term>Motifs d'acides aminés</term><term>Peptides ()</term><term>Protéines de fusion virale ()</term><term>Protéines de l'enveloppe virale ()</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Similitude de séquences d'acides aminés</term><term>Souris</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</term><term>Virus de l'hépatite murine (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Glycoproteins</term><term>Peptides</term><term>Viral Envelope Proteins</term><term>Viral Fusion Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Hemagglutinin Glycoproteins, Influenza Virus</term><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Coronavirus</term><term>Escherichia coli</term><term>Murine hepatitis virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Coronavirus</term><term>Escherichia coli</term><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term><term>Virus de l'hépatite murine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term><term>Amino Acid Sequence</term><term>Animals</term><term>Crystallography, X-Ray</term><term>Dimerization</term><term>Hydrogen-Ion Concentration</term><term>Membrane Fusion</term><term>Mice</term><term>Models, Biological</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Protein Binding</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term><term>Sequence Homology, Amino Acid</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Concentration en ions d'hydrogène</term><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Dimérisation</term><term>Données de séquences moléculaires</term><term>Fusion membranaire</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires</term><term>Liaison aux protéines</term><term>Modèles biologiques</term><term>Modèles moléculaires</term><term>Motifs d'acides aminés</term><term>Peptides</term><term>Protéines de fusion virale</term><term>Protéines de l'enveloppe virale</term><term>Similitude de séquences d'acides aminés</term><term>Souris</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The surface transmembrane glycoprotein is responsible for mediating virion attachment to cell and subsequent virus-cell membrane fusion. However, the molecular mechanisms for the viral entry of coronaviruses remain poorly understood. The crystal structure of the fusion core of mouse hepatitis virus S protein, which represents the first fusion core structure of any coronavirus, reveals a central hydrophobic coiled coil trimer surrounded by three helices in an oblique, antiparallel manner. This structure shares significant similarity with both the low pH-induced conformation of influenza hemagglutinin and fusion core of HIV gp41, indicating that the structure represents a fusion-active state formed after several conformational changes. Our results also indicate that the mechanisms for the viral fusion of coronaviruses are similar to those of influenza virus and HIV. The coiled coil structure has unique features, which are different from other viral fusion cores. Highly conserved heptad repeat 1 (HR1) and HR2 regions in coronavirus spike proteins indicate a similar three-dimensional structure among these fusion cores and common mechanisms for the viral fusion. We have proposed the binding regions of HR1 and HR2 of other coronaviruses and a structure model of their fusion core based on our mouse hepatitis virus fusion core structure and sequence alignment. Drug discovery strategies aimed at inhibiting viral entry by blocking hairpin formation may be applied to the inhibition of a number of emerging infectious diseases, including severe acute respiratory syndrome.</div></front></TEI><affiliations><list><country><li>République populaire de Chine</li></country><settlement><li>Pékin</li></settlement></list><tree><noCountry><name sortKey="Bai, Zhihong" sort="Bai, Zhihong" uniqKey="Bai Z" first="Zhihong" last="Bai">Zhihong Bai</name><name sortKey="Gao, George F" sort="Gao, George F" uniqKey="Gao G" first="George F" last="Gao">George F. Gao</name><name sortKey="Li, Xu" sort="Li, Xu" uniqKey="Li X" first="Xu" last="Li">Xu Li</name><name sortKey="Liu, Yiwei" sort="Liu, Yiwei" uniqKey="Liu Y" first="Yiwei" last="Liu">Yiwei Liu</name><name sortKey="Lou, Zhiyong" sort="Lou, Zhiyong" uniqKey="Lou Z" first="Zhiyong" last="Lou">Zhiyong Lou</name><name sortKey="Pang, Hai" sort="Pang, Hai" uniqKey="Pang H" first="Hai" last="Pang">Hai Pang</name><name sortKey="Qin, Lan" sort="Qin, Lan" uniqKey="Qin L" first="Lan" last="Qin">Lan Qin</name><name sortKey="Rao, Zihe" sort="Rao, Zihe" uniqKey="Rao Z" first="Zihe" last="Rao">Zihe Rao</name><name sortKey="Tien, Po" sort="Tien, Po" uniqKey="Tien P" first="Po" last="Tien">Po Tien</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Xu, Yanhui" sort="Xu, Yanhui" uniqKey="Xu Y" first="Yanhui" last="Xu">Yanhui Xu</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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