Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus.
Identifieur interne : 002027 ( Main/Exploration ); précédent : 002026; suivant : 002028Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus.
Auteurs : Yaoqing Chen [États-Unis] ; Kanagalaghatta R. Rajashankar ; Yang Yang ; Sudhakar S. Agnihothram ; Chang Liu ; Yi-Lun Lin ; Ralph S. Baric ; Fang LiSource :
- Journal of virology [ 1098-5514 ] ; 2013.
Descripteurs français
- KwdFr :
- Conformation des protéines, Coronavirus (physiologie), Cristallographie aux rayons X, Dipeptidyl peptidase 4 (métabolisme), Données de séquences moléculaires, Humains, Interactions hôte-pathogène, Moyen Orient, Protéines virales (), Protéines virales (métabolisme), Similitude de séquences d'acides aminés, Syndrome, Séquence d'acides aminés, Virus de la leucémie murine (génétique).
- MESH :
- génétique : Virus de la leucémie murine.
- métabolisme : Dipeptidyl peptidase 4, Protéines virales.
- physiologie : Coronavirus.
- Conformation des protéines, Cristallographie aux rayons X, Données de séquences moléculaires, Humains, Interactions hôte-pathogène, Moyen Orient, Protéines virales, Similitude de séquences d'acides aminés, Syndrome, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Coronavirus (physiology), Crystallography, X-Ray, Dipeptidyl Peptidase 4 (metabolism), Host-Pathogen Interactions, Humans, Leukemia Virus, Murine (genetics), Middle East, Molecular Sequence Data, Protein Conformation, Sequence Homology, Amino Acid, Syndrome, Viral Proteins (chemistry), Viral Proteins (metabolism).
- MESH :
- chemical , chemistry : Viral Proteins.
- chemical , metabolism : Dipeptidyl Peptidase 4, Viral Proteins.
- geographic : Middle East.
- genetics : Leukemia Virus, Murine.
- physiology : Coronavirus.
- Amino Acid Sequence, Crystallography, X-Ray, Host-Pathogen Interactions, Humans, Molecular Sequence Data, Protein Conformation, Sequence Homology, Amino Acid, Syndrome.
Abstract
The newly emerged Middle East respiratory syndrome coronavirus (MERS-CoV) has infected at least 77 people, with a fatality rate of more than 50%. Alarmingly, the virus demonstrates the capability of human-to-human transmission, raising the possibility of global spread and endangering world health and economy. Here we have identified the receptor-binding domain (RBD) from the MERS-CoV spike protein and determined its crystal structure. This study also presents a structural comparison of MERS-CoV RBD with other coronavirus RBDs, successfully positioning MERS-CoV on the landscape of coronavirus evolution and providing insights into receptor binding by MERS-CoV. Furthermore, we found that MERS-CoV RBD functions as an effective entry inhibitor of MERS-CoV. The identified MERS-CoV RBD may also serve as a potential candidate for MERS-CoV subunit vaccines. Overall, this study enhances our understanding of the evolution of coronavirus RBDs, provides insights into receptor recognition by MERS-CoV, and may help control the transmission of MERS-CoV in humans.
DOI: 10.1128/JVI.01756-13
PubMed: 23903833
Affiliations:
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Le document en format XML
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Rajashankar</name></author><author><name sortKey="Yang, Yang" sort="Yang, Yang" uniqKey="Yang Y" first="Yang" last="Yang">Yang Yang</name></author><author><name sortKey="Agnihothram, Sudhakar S" sort="Agnihothram, Sudhakar S" uniqKey="Agnihothram S" first="Sudhakar S" last="Agnihothram">Sudhakar S. Agnihothram</name></author><author><name sortKey="Liu, Chang" sort="Liu, Chang" uniqKey="Liu C" first="Chang" last="Liu">Chang Liu</name></author><author><name sortKey="Lin, Yi Lun" sort="Lin, Yi Lun" uniqKey="Lin Y" first="Yi-Lun" last="Lin">Yi-Lun Lin</name></author><author><name sortKey="Baric, Ralph S" sort="Baric, Ralph S" uniqKey="Baric R" first="Ralph S" last="Baric">Ralph S. Baric</name></author><author><name sortKey="Li, Fang" sort="Li, Fang" uniqKey="Li F" first="Fang" last="Li">Fang Li</name></author></analytic><series><title level="j">Journal of virology</title><idno type="eISSN">1098-5514</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Coronavirus (physiology)</term><term>Crystallography, X-Ray</term><term>Dipeptidyl Peptidase 4 (metabolism)</term><term>Host-Pathogen Interactions</term><term>Humans</term><term>Leukemia Virus, Murine (genetics)</term><term>Middle East</term><term>Molecular Sequence Data</term><term>Protein Conformation</term><term>Sequence Homology, Amino Acid</term><term>Syndrome</term><term>Viral Proteins (chemistry)</term><term>Viral Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Conformation des protéines</term><term>Coronavirus (physiologie)</term><term>Cristallographie aux rayons X</term><term>Dipeptidyl peptidase 4 (métabolisme)</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Interactions hôte-pathogène</term><term>Moyen Orient</term><term>Protéines virales ()</term><term>Protéines virales (métabolisme)</term><term>Similitude de séquences d'acides aminés</term><term>Syndrome</term><term>Séquence d'acides aminés</term><term>Virus de la leucémie murine (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Dipeptidyl Peptidase 4</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="geographic" xml:lang="en"><term>Middle East</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Leukemia Virus, Murine</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Virus de la leucémie murine</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Dipeptidyl peptidase 4</term><term>Protéines virales</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Coronavirus</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Coronavirus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Crystallography, X-Ray</term><term>Host-Pathogen Interactions</term><term>Humans</term><term>Molecular Sequence Data</term><term>Protein Conformation</term><term>Sequence Homology, Amino Acid</term><term>Syndrome</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Interactions hôte-pathogène</term><term>Moyen Orient</term><term>Protéines virales</term><term>Similitude de séquences d'acides aminés</term><term>Syndrome</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The newly emerged Middle East respiratory syndrome coronavirus (MERS-CoV) has infected at least 77 people, with a fatality rate of more than 50%. Alarmingly, the virus demonstrates the capability of human-to-human transmission, raising the possibility of global spread and endangering world health and economy. Here we have identified the receptor-binding domain (RBD) from the MERS-CoV spike protein and determined its crystal structure. This study also presents a structural comparison of MERS-CoV RBD with other coronavirus RBDs, successfully positioning MERS-CoV on the landscape of coronavirus evolution and providing insights into receptor binding by MERS-CoV. Furthermore, we found that MERS-CoV RBD functions as an effective entry inhibitor of MERS-CoV. The identified MERS-CoV RBD may also serve as a potential candidate for MERS-CoV subunit vaccines. Overall, this study enhances our understanding of the evolution of coronavirus RBDs, provides insights into receptor recognition by MERS-CoV, and may help control the transmission of MERS-CoV in humans. </div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Minnesota</li></region></list><tree><noCountry><name sortKey="Agnihothram, Sudhakar S" sort="Agnihothram, Sudhakar S" uniqKey="Agnihothram S" first="Sudhakar S" last="Agnihothram">Sudhakar S. Agnihothram</name><name sortKey="Baric, Ralph S" sort="Baric, Ralph S" uniqKey="Baric R" first="Ralph S" last="Baric">Ralph S. Baric</name><name sortKey="Li, Fang" sort="Li, Fang" uniqKey="Li F" first="Fang" last="Li">Fang Li</name><name sortKey="Lin, Yi Lun" sort="Lin, Yi Lun" uniqKey="Lin Y" first="Yi-Lun" last="Lin">Yi-Lun Lin</name><name sortKey="Liu, Chang" sort="Liu, Chang" uniqKey="Liu C" first="Chang" last="Liu">Chang Liu</name><name sortKey="Rajashankar, Kanagalaghatta R" sort="Rajashankar, Kanagalaghatta R" uniqKey="Rajashankar K" first="Kanagalaghatta R" last="Rajashankar">Kanagalaghatta R. Rajashankar</name><name sortKey="Yang, Yang" sort="Yang, Yang" uniqKey="Yang Y" first="Yang" last="Yang">Yang Yang</name></noCountry><country name="États-Unis"><region name="Minnesota"><name sortKey="Chen, Yaoqing" sort="Chen, Yaoqing" uniqKey="Chen Y" first="Yaoqing" last="Chen">Yaoqing Chen</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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