Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4.
Identifieur interne : 001855 ( Main/Exploration ); précédent : 001854; suivant : 001856Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4.
Auteurs : Nianshuang Wang [République populaire de Chine] ; Xuanling Shi ; Liwei Jiang ; Senyan Zhang ; Dongli Wang ; Pei Tong ; Dongxing Guo ; Lili Fu ; Ye Cui ; Xi Liu ; Kelly C. Arledge ; Ying-Hua Chen ; Linqi Zhang ; Xinquan WangSource :
- Cell research [ 1748-7838 ] ; 2013.
Descripteurs français
- KwdFr :
- Animaux, Cellules Sf9, Coronavirus (métabolisme), Dipeptidyl peptidase 4 (), Dipeptidyl peptidase 4 (génétique), Dipeptidyl peptidase 4 (métabolisme), Humains, Liaison aux protéines, Protéines virales (), Protéines virales (génétique), Protéines virales (métabolisme), Pénétration virale, Sites de fixation, Spodoptera, Structure tertiaire des protéines, Substitution d'acide aminé, Virus du SRAS (métabolisme).
- MESH :
- génétique : Dipeptidyl peptidase 4, Protéines virales.
- métabolisme : Coronavirus, Dipeptidyl peptidase 4, Protéines virales, Virus du SRAS.
- Animaux, Cellules Sf9, Dipeptidyl peptidase 4, Humains, Liaison aux protéines, Protéines virales, Pénétration virale, Sites de fixation, Spodoptera, Structure tertiaire des protéines, Substitution d'acide aminé.
English descriptors
- KwdEn :
- Amino Acid Substitution, Animals, Binding Sites, Coronavirus (metabolism), Dipeptidyl Peptidase 4 (chemistry), Dipeptidyl Peptidase 4 (genetics), Dipeptidyl Peptidase 4 (metabolism), Humans, Protein Binding, Protein Structure, Tertiary, SARS Virus (metabolism), Sf9 Cells, Spodoptera, Viral Proteins (chemistry), Viral Proteins (genetics), Viral Proteins (metabolism), Virus Internalization.
- MESH :
- chemical , chemistry : Dipeptidyl Peptidase 4, Viral Proteins.
- chemical , genetics : Dipeptidyl Peptidase 4, Viral Proteins.
- metabolism : Coronavirus, Dipeptidyl Peptidase 4, SARS Virus, Viral Proteins.
- Amino Acid Substitution, Animals, Binding Sites, Humans, Protein Binding, Protein Structure, Tertiary, Sf9 Cells, Spodoptera, Virus Internalization.
Abstract
The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV) targets the cellular receptor, dipeptidyl peptidase 4 (DPP4). Sequence comparison and modeling analysis have revealed a putative receptor-binding domain (RBD) on the viral spike, which mediates this interaction. We report the 3.0 Å-resolution crystal structure of MERS-CoV RBD bound to the extracellular domain of human DPP4. Our results show that MERS-CoV RBD consists of a core and a receptor-binding subdomain. The receptor-binding subdomain interacts with DPP4 β-propeller but not its intrinsic hydrolase domain. MERS-CoV RBD and related SARS-CoV RBD share a high degree of structural similarity in their core subdomains, but are notably divergent in the receptor-binding subdomain. Mutagenesis studies have identified several key residues in the receptor-binding subdomain that are critical for viral binding to DPP4 and entry into the target cell. The atomic details at the interface between MERS-CoV RBD and DPP4 provide structural understanding of the virus and receptor interaction, which can guide development of therapeutics and vaccines against MERS-CoV infection.
DOI: 10.1038/cr.2013.92
PubMed: 23835475
Affiliations:
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Le document en format XML
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Arledge</name></author><author><name sortKey="Chen, Ying Hua" sort="Chen, Ying Hua" uniqKey="Chen Y" first="Ying-Hua" last="Chen">Ying-Hua Chen</name></author><author><name sortKey="Zhang, Linqi" sort="Zhang, Linqi" uniqKey="Zhang L" first="Linqi" last="Zhang">Linqi Zhang</name></author><author><name sortKey="Wang, Xinquan" sort="Wang, Xinquan" uniqKey="Wang X" first="Xinquan" last="Wang">Xinquan Wang</name></author></analytic><series><title level="j">Cell research</title><idno type="eISSN">1748-7838</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 Substitution</term><term>Animals</term><term>Binding Sites</term><term>Coronavirus (metabolism)</term><term>Dipeptidyl Peptidase 4 (chemistry)</term><term>Dipeptidyl Peptidase 4 (genetics)</term><term>Dipeptidyl Peptidase 4 (metabolism)</term><term>Humans</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>SARS Virus (metabolism)</term><term>Sf9 Cells</term><term>Spodoptera</term><term>Viral Proteins (chemistry)</term><term>Viral Proteins (genetics)</term><term>Viral Proteins (metabolism)</term><term>Virus Internalization</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Cellules Sf9</term><term>Coronavirus (métabolisme)</term><term>Dipeptidyl peptidase 4 ()</term><term>Dipeptidyl peptidase 4 (génétique)</term><term>Dipeptidyl peptidase 4 (métabolisme)</term><term>Humains</term><term>Liaison aux protéines</term><term>Protéines virales ()</term><term>Protéines virales (génétique)</term><term>Protéines virales (métabolisme)</term><term>Pénétration virale</term><term>Sites de fixation</term><term>Spodoptera</term><term>Structure tertiaire des protéines</term><term>Substitution d'acide aminé</term><term>Virus du SRAS (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Dipeptidyl Peptidase 4</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Dipeptidyl Peptidase 4</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Dipeptidyl peptidase 4</term><term>Protéines virales</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Coronavirus</term><term>Dipeptidyl Peptidase 4</term><term>SARS Virus</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Coronavirus</term><term>Dipeptidyl peptidase 4</term><term>Protéines virales</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Substitution</term><term>Animals</term><term>Binding Sites</term><term>Humans</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>Sf9 Cells</term><term>Spodoptera</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules Sf9</term><term>Dipeptidyl peptidase 4</term><term>Humains</term><term>Liaison aux protéines</term><term>Protéines virales</term><term>Pénétration virale</term><term>Sites de fixation</term><term>Spodoptera</term><term>Structure tertiaire des protéines</term><term>Substitution d'acide aminé</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV) targets the cellular receptor, dipeptidyl peptidase 4 (DPP4). Sequence comparison and modeling analysis have revealed a putative receptor-binding domain (RBD) on the viral spike, which mediates this interaction. We report the 3.0 Å-resolution crystal structure of MERS-CoV RBD bound to the extracellular domain of human DPP4. Our results show that MERS-CoV RBD consists of a core and a receptor-binding subdomain. The receptor-binding subdomain interacts with DPP4 β-propeller but not its intrinsic hydrolase domain. MERS-CoV RBD and related SARS-CoV RBD share a high degree of structural similarity in their core subdomains, but are notably divergent in the receptor-binding subdomain. Mutagenesis studies have identified several key residues in the receptor-binding subdomain that are critical for viral binding to DPP4 and entry into the target cell. The atomic details at the interface between MERS-CoV RBD and DPP4 provide structural understanding of the virus and receptor interaction, which can guide development of therapeutics and vaccines against MERS-CoV infection.</div></front></TEI><affiliations><list><country><li>République populaire de Chine</li></country><settlement><li>Pékin</li></settlement></list><tree><noCountry><name sortKey="Arledge, Kelly C" sort="Arledge, Kelly C" uniqKey="Arledge K" first="Kelly C" last="Arledge">Kelly C. Arledge</name><name sortKey="Chen, Ying Hua" sort="Chen, Ying Hua" uniqKey="Chen Y" first="Ying-Hua" last="Chen">Ying-Hua Chen</name><name sortKey="Cui, Ye" sort="Cui, Ye" uniqKey="Cui Y" first="Ye" last="Cui">Ye Cui</name><name sortKey="Fu, Lili" sort="Fu, Lili" uniqKey="Fu L" first="Lili" last="Fu">Lili Fu</name><name sortKey="Guo, Dongxing" sort="Guo, Dongxing" uniqKey="Guo D" first="Dongxing" last="Guo">Dongxing Guo</name><name sortKey="Jiang, Liwei" sort="Jiang, Liwei" uniqKey="Jiang L" first="Liwei" last="Jiang">Liwei Jiang</name><name sortKey="Liu, Xi" sort="Liu, Xi" uniqKey="Liu X" first="Xi" last="Liu">Xi Liu</name><name sortKey="Shi, Xuanling" sort="Shi, Xuanling" uniqKey="Shi X" first="Xuanling" last="Shi">Xuanling Shi</name><name sortKey="Tong, Pei" sort="Tong, Pei" uniqKey="Tong P" first="Pei" last="Tong">Pei Tong</name><name sortKey="Wang, Dongli" sort="Wang, Dongli" uniqKey="Wang D" first="Dongli" last="Wang">Dongli Wang</name><name sortKey="Wang, Xinquan" sort="Wang, Xinquan" uniqKey="Wang X" first="Xinquan" last="Wang">Xinquan Wang</name><name sortKey="Zhang, Linqi" sort="Zhang, Linqi" uniqKey="Zhang L" first="Linqi" last="Zhang">Linqi Zhang</name><name sortKey="Zhang, Senyan" sort="Zhang, Senyan" uniqKey="Zhang S" first="Senyan" last="Zhang">Senyan Zhang</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Wang, Nianshuang" sort="Wang, Nianshuang" uniqKey="Wang N" first="Nianshuang" last="Wang">Nianshuang Wang</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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