Molecular basis of binding between novel human coronavirus MERS-CoV and its receptor CD26.
Identifieur interne : 002706 ( Ncbi/Curation ); précédent : 002705; suivant : 002707Molecular basis of binding between novel human coronavirus MERS-CoV and its receptor CD26.
Auteurs : Guangwen Lu [République populaire de Chine] ; Yawei Hu ; Qihui Wang ; Jianxun Qi ; Feng Gao ; Yan Li ; Yanfang Zhang ; Wei Zhang ; Yuan Yuan ; Jinku Bao ; Buchang Zhang ; Yi Shi ; Jinghua Yan ; George F. GaoSource :
- Nature [ 1476-4687 ] ; 2013.
Descripteurs français
- KwdFr :
- Attachement viral, Coronavirus (), Coronavirus (génétique), Coronavirus (métabolisme), Dipeptidyl peptidase 4 (), Dipeptidyl peptidase 4 (métabolisme), Humains, Liaison aux protéines, Motifs et domaines d'intéraction protéique (génétique), Récepteurs viraux (), Récepteurs viraux (métabolisme), Structure tertiaire des protéines (génétique), Séquence conservée (génétique).
- MESH :
- génétique : Coronavirus, Motifs et domaines d'intéraction protéique, Structure tertiaire des protéines, Séquence conservée.
- métabolisme : Coronavirus, Dipeptidyl peptidase 4, Récepteurs viraux.
- Attachement viral, Coronavirus, Dipeptidyl peptidase 4, Humains, Liaison aux protéines, Récepteurs viraux.
English descriptors
- KwdEn :
- Conserved Sequence (genetics), Coronavirus (chemistry), Coronavirus (genetics), Coronavirus (metabolism), Dipeptidyl Peptidase 4 (chemistry), Dipeptidyl Peptidase 4 (metabolism), Humans, Protein Binding, Protein Interaction Domains and Motifs (genetics), Protein Structure, Tertiary (genetics), Receptors, Virus (chemistry), Receptors, Virus (metabolism), Virus Attachment.
- MESH :
- chemical , chemistry : Dipeptidyl Peptidase 4, Receptors, Virus.
- chemistry : Coronavirus.
- genetics : Conserved Sequence, Coronavirus, Protein Interaction Domains and Motifs, Protein Structure, Tertiary.
- metabolism : Coronavirus, Dipeptidyl Peptidase 4, Receptors, Virus.
- Humans, Protein Binding, Virus Attachment.
Abstract
The newly emergent Middle East respiratory syndrome coronavirus (MERS-CoV) can cause severe pulmonary disease in humans, representing the second example of a highly pathogenic coronavirus, the first being SARS-CoV. CD26 (also known as dipeptidyl peptidase 4, DPP4) was recently identified as the cellular receptor for MERS-CoV. The engagement of the MERS-CoV spike protein with CD26 mediates viral attachment to host cells and virus-cell fusion, thereby initiating infection. Here we delineate the molecular basis of this specific interaction by presenting the first crystal structures of both the free receptor binding domain (RBD) of the MERS-CoV spike protein and its complex with CD26. Furthermore, binding between the RBD and CD26 is measured using real-time surface plasmon resonance with a dissociation constant of 16.7 nM. The viral RBD is composed of a core subdomain homologous to that of the SARS-CoV spike protein, and a unique strand-dominated external receptor binding motif that recognizes blades IV and V of the CD26 β-propeller. The atomic details at the interface between the two binding entities reveal a surprising protein-protein contact mediated mainly by hydrophilic residues. Sequence alignment indicates, among betacoronaviruses, a possible structural conservation for the region homologous to the MERS-CoV RBD core, but a high variation in the external receptor binding motif region for virus-specific pathogenesis such as receptor recognition.
DOI: 10.1038/nature12328
PubMed: 23831647
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pubmed:23831647Le document en format XML
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Gao</name></author></analytic><series><title level="j">Nature</title><idno type="eISSN">1476-4687</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Conserved Sequence (genetics)</term><term>Coronavirus (chemistry)</term><term>Coronavirus (genetics)</term><term>Coronavirus (metabolism)</term><term>Dipeptidyl Peptidase 4 (chemistry)</term><term>Dipeptidyl Peptidase 4 (metabolism)</term><term>Humans</term><term>Protein Binding</term><term>Protein Interaction Domains and Motifs (genetics)</term><term>Protein Structure, Tertiary (genetics)</term><term>Receptors, Virus (chemistry)</term><term>Receptors, Virus (metabolism)</term><term>Virus Attachment</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Attachement viral</term><term>Coronavirus ()</term><term>Coronavirus (génétique)</term><term>Coronavirus (métabolisme)</term><term>Dipeptidyl peptidase 4 ()</term><term>Dipeptidyl peptidase 4 (métabolisme)</term><term>Humains</term><term>Liaison aux protéines</term><term>Motifs et domaines d'intéraction protéique (génétique)</term><term>Récepteurs viraux ()</term><term>Récepteurs viraux (métabolisme)</term><term>Structure tertiaire des protéines (génétique)</term><term>Séquence conservée (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Dipeptidyl Peptidase 4</term><term>Receptors, Virus</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Coronavirus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Conserved Sequence</term><term>Coronavirus</term><term>Protein Interaction Domains and Motifs</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Coronavirus</term><term>Motifs et domaines d'intéraction protéique</term><term>Structure tertiaire des protéines</term><term>Séquence conservée</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Coronavirus</term><term>Dipeptidyl Peptidase 4</term><term>Receptors, Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Coronavirus</term><term>Dipeptidyl peptidase 4</term><term>Récepteurs viraux</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Protein Binding</term><term>Virus Attachment</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Attachement viral</term><term>Coronavirus</term><term>Dipeptidyl peptidase 4</term><term>Humains</term><term>Liaison aux protéines</term><term>Récepteurs viraux</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The newly emergent Middle East respiratory syndrome coronavirus (MERS-CoV) can cause severe pulmonary disease in humans, representing the second example of a highly pathogenic coronavirus, the first being SARS-CoV. CD26 (also known as dipeptidyl peptidase 4, DPP4) was recently identified as the cellular receptor for MERS-CoV. The engagement of the MERS-CoV spike protein with CD26 mediates viral attachment to host cells and virus-cell fusion, thereby initiating infection. Here we delineate the molecular basis of this specific interaction by presenting the first crystal structures of both the free receptor binding domain (RBD) of the MERS-CoV spike protein and its complex with CD26. Furthermore, binding between the RBD and CD26 is measured using real-time surface plasmon resonance with a dissociation constant of 16.7 nM. The viral RBD is composed of a core subdomain homologous to that of the SARS-CoV spike protein, and a unique strand-dominated external receptor binding motif that recognizes blades IV and V of the CD26 β-propeller. The atomic details at the interface between the two binding entities reveal a surprising protein-protein contact mediated mainly by hydrophilic residues. Sequence alignment indicates, among betacoronaviruses, a possible structural conservation for the region homologous to the MERS-CoV RBD core, but a high variation in the external receptor binding motif region for virus-specific pathogenesis such as receptor recognition. </div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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