Identification of residues on human receptor DPP4 critical for MERS-CoV binding and entry
Identifieur interne : 001C28 ( Main/Exploration ); précédent : 001C27; suivant : 001C29Identification of residues on human receptor DPP4 critical for MERS-CoV binding and entry
Auteurs : Wenfei Song [République populaire de Chine] ; Ying Wang [République populaire de Chine] ; Nianshuang Wang [République populaire de Chine] ; Dongli Wang [République populaire de Chine] ; Jianying Guo [République populaire de Chine] ; Lili Fu [République populaire de Chine] ; Xuanling Shi [République populaire de Chine]Source :
- Virology [ 0042-6822 ] ; 2014.
Descripteurs français
- KwdFr :
- Animaux, Conformation des protéines, Coronavirus du syndrome respiratoire du Moyen-Orient (physiologie), Dipeptidyl peptidase 4 (génétique), Dipeptidyl peptidase 4 (métabolisme), Données de séquences moléculaires, Humains, Lignée cellulaire, Modèles moléculaires, Pénétration virale, Régulation de l'expression des gènes viraux (physiologie), Séquence d'acides aminés.
- MESH :
- génétique : Dipeptidyl peptidase 4.
- métabolisme : Dipeptidyl peptidase 4.
- physiologie : Coronavirus du syndrome respiratoire du Moyen-Orient, Régulation de l'expression des gènes viraux.
- Animaux, Conformation des protéines, Données de séquences moléculaires, Humains, Lignée cellulaire, Modèles moléculaires, Pénétration virale, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Cell Line, Dipeptidyl Peptidase 4 (genetics), Dipeptidyl Peptidase 4 (metabolism), Gene Expression Regulation, Viral (physiology), Humans, Insecta, Middle East Respiratory Syndrome Coronavirus (physiology), Models, Molecular, Molecular Sequence Data, Protein Conformation, Virus Internalization.
- MESH :
- chemical , genetics : Dipeptidyl Peptidase 4.
- chemical , metabolism : Dipeptidyl Peptidase 4.
- physiology : Gene Expression Regulation, Viral, Middle East Respiratory Syndrome Coronavirus.
- Amino Acid Sequence, Animals, Cell Line, Humans, Insecta, Models, Molecular, Molecular Sequence Data, Protein Conformation, Virus Internalization.
Abstract
Middle East respiratory syndrome coronavirus (MERS-CoV) infects host cells through binding the receptor binding domain (RBD) on its spike glycoprotein to human receptor dipeptidyl peptidase 4 (hDPP4). Here, we report identification of critical residues on hDPP4 for RBD binding and virus entry through analysis of a panel of hDPP4 mutants. Based on the RBD–hDPP4 crystal structure we reported, the mutated residues were located at the interface between RBD and hDPP4, which potentially changed the polarity, hydrophobic or hydrophilic properties of hDPP4, thereby interfering or disrupting their interaction with RBD. Using surface plasmon resonance (SPR) binding analysis and pseudovirus infection assay, we showed that several residues in hDPP4–RBD binding interface were important on hDPP4–RBD binding and viral entry. These results provide atomic insights into the features of interactions between hDPP4 and MERS-CoV RBD, and also provide potential explanation for cellular and species tropism of MERS-CoV infection.
Url:
DOI: 10.1016/j.virol.2014.10.006
PubMed: 25461530
PubMed Central: 7112127
Affiliations:
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Le document en format XML
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School of Medicine, Tsinghua University, Beijing 100084</wicri:regionArea><placeName><settlement type="city">Pékin</settlement></placeName></affiliation></author></analytic><series><title level="j">Virology</title><idno type="ISSN">0042-6822</idno><idno type="eISSN">1096-0341</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Cell Line</term><term>Dipeptidyl Peptidase 4 (genetics)</term><term>Dipeptidyl Peptidase 4 (metabolism)</term><term>Gene Expression Regulation, Viral (physiology)</term><term>Humans</term><term>Insecta</term><term>Middle East Respiratory Syndrome Coronavirus (physiology)</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Protein Conformation</term><term>Virus Internalization</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Conformation des protéines</term><term>Coronavirus du syndrome respiratoire du Moyen-Orient (physiologie)</term><term>Dipeptidyl peptidase 4 (génétique)</term><term>Dipeptidyl peptidase 4 (métabolisme)</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Lignée cellulaire</term><term>Modèles moléculaires</term><term>Pénétration virale</term><term>Régulation de l'expression des gènes viraux (physiologie)</term><term>Séquence d'acides aminés</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Dipeptidyl Peptidase 4</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Dipeptidyl Peptidase 4</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Dipeptidyl peptidase 4</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Dipeptidyl peptidase 4</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Coronavirus du syndrome respiratoire du Moyen-Orient</term><term>Régulation de l'expression des gènes viraux</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Gene Expression Regulation, Viral</term><term>Middle East Respiratory Syndrome Coronavirus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Cell Line</term><term>Humans</term><term>Insecta</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Protein Conformation</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Conformation des protéines</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Lignée cellulaire</term><term>Modèles moléculaires</term><term>Pénétration virale</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Middle East respiratory syndrome coronavirus (MERS-CoV) infects host cells through binding the receptor binding domain (RBD) on its spike glycoprotein to human receptor dipeptidyl peptidase 4 (hDPP4). Here, we report identification of critical residues on hDPP4 for RBD binding and virus entry through analysis of a panel of hDPP4 mutants. Based on the RBD–hDPP4 crystal structure we reported, the mutated residues were located at the interface between RBD and hDPP4, which potentially changed the polarity, hydrophobic or hydrophilic properties of hDPP4, thereby interfering or disrupting their interaction with RBD. Using surface plasmon resonance (SPR) binding analysis and pseudovirus infection assay, we showed that several residues in hDPP4–RBD binding interface were important on hDPP4–RBD binding and viral entry. These results provide atomic insights into the features of interactions between hDPP4 and MERS-CoV RBD, and also provide potential explanation for cellular and species tropism of MERS-CoV infection.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Chen, Y" uniqKey="Chen Y">Y. Chen</name></author><author><name sortKey="Rajashankar, K R" uniqKey="Rajashankar K">K.R. Rajashankar</name></author><author><name sortKey="Yang, Y" uniqKey="Yang Y">Y. Yang</name></author><author><name sortKey="Agnihothram, S S" uniqKey="Agnihothram S">S.S. Agnihothram</name></author><author><name sortKey="Liu, C" uniqKey="Liu C">C. Liu</name></author><author><name sortKey="Lin, Y L" uniqKey="Lin Y">Y.L. Lin</name></author><author><name sortKey="Baric, R S" uniqKey="Baric R">R.S. Baric</name></author><author><name sortKey="Li, F" uniqKey="Li F">F. Li</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Coleman, C M" uniqKey="Coleman C">C.M. Coleman</name></author><author><name sortKey="Matthews, K L" uniqKey="Matthews K">K.L. Matthews</name></author><author><name sortKey="Goicochea, L" uniqKey="Goicochea L">L. Goicochea</name></author><author><name sortKey="Frieman, M B" uniqKey="Frieman M">M.B. 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Perlman</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list><country><li>République populaire de Chine</li></country><settlement><li>Pékin</li></settlement></list><tree><country name="République populaire de Chine"><noRegion><name sortKey="Song, Wenfei" sort="Song, Wenfei" uniqKey="Song W" first="Wenfei" last="Song">Wenfei Song</name></noRegion><name sortKey="Fu, Lili" sort="Fu, Lili" uniqKey="Fu L" first="Lili" last="Fu">Lili Fu</name><name sortKey="Guo, Jianying" sort="Guo, Jianying" uniqKey="Guo J" first="Jianying" last="Guo">Jianying Guo</name><name sortKey="Shi, Xuanling" sort="Shi, Xuanling" uniqKey="Shi X" first="Xuanling" last="Shi">Xuanling Shi</name><name sortKey="Wang, Dongli" sort="Wang, Dongli" uniqKey="Wang D" first="Dongli" last="Wang">Dongli Wang</name><name sortKey="Wang, Nianshuang" sort="Wang, Nianshuang" uniqKey="Wang N" first="Nianshuang" last="Wang">Nianshuang Wang</name><name sortKey="Wang, Ying" sort="Wang, Ying" uniqKey="Wang Y" first="Ying" last="Wang">Ying Wang</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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