Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4
Identifieur interne : 001F00 ( Main/Exploration ); précédent : 001E99; suivant : 001F01Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4
Auteurs : Nianshuang Wang [République populaire de Chine] ; Xuanling Shi [République populaire de Chine] ; Liwei Jiang [République populaire de Chine] ; Senyan Zhang [République populaire de Chine] ; Dongli Wang [République populaire de Chine] ; Pei Tong [République populaire de Chine] ; Dongxing Guo [République populaire de Chine] ; Lili Fu [République populaire de Chine] ; Ye Cui [République populaire de Chine] ; Xi Liu [République populaire de Chine] ; Kelly C. Arledge [République populaire de Chine] ; Ying-Hua Chen [République populaire de Chine] ; Linqi Zhang [République populaire de Chine] ; Xinquan Wang [République populaire de Chine]Source :
- Cell Research [ 1001-0602 ] ; 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.
The online version of this article (doi:10.1038/cr.2013.92) contains supplementary material, which is available to authorized users.
Url:
DOI: 10.1038/cr.2013.92
PubMed: 23835475
PubMed Central: 3731569
Affiliations:
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Le document en format XML
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School of Life Sciences, Tsinghua University,</institution></institution-wrap>Beijing, 100084 China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Beijing</wicri:regionArea></affiliation></author><author><name sortKey="Zhang, Linqi" sort="Zhang, Linqi" uniqKey="Zhang L" first="Linqi" last="Zhang">Linqi Zhang</name><affiliation wicri:level="1"><nlm:aff id="Aff2"><institution-wrap><institution-id institution-id-type="GRID">grid.12527.33</institution-id><institution-id institution-id-type="ISNI">0000 0001 0662 3178</institution-id><institution>Comprehensive AIDS Research Center, Research Center for Public Health, School of Medicine, Tsinghua University,</institution></institution-wrap>Beijing, 100084 China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Beijing</wicri:regionArea></affiliation></author><author><name sortKey="Wang, Xinquan" sort="Wang, Xinquan" uniqKey="Wang X" first="Xinquan" last="Wang">Xinquan Wang</name><affiliation wicri:level="1"><nlm:aff id="Aff1"><institution-wrap><institution-id institution-id-type="GRID">grid.12527.33</institution-id><institution-id institution-id-type="ISNI">0000 0001 0662 3178</institution-id><institution>Ministry of Education Key Laboratory of Protein Science, Center for Structural Biology, School of Life Sciences, Tsinghua University,</institution></institution-wrap>Beijing, 100084 China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Beijing</wicri:regionArea></affiliation></author></analytic><series><title level="j">Cell Research</title><idno type="ISSN">1001-0602</idno><idno type="eISSN">1748-7838</idno><imprint><date when="2013">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"><p id="Par1">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.</p><sec><title>Supplementary information</title><p>The online version of this article (doi:10.1038/cr.2013.92) contains supplementary material, which is available to authorized users.</p></sec></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Bermingham, A" uniqKey="Bermingham A">A Bermingham</name></author><author><name sortKey="Chand, Ma" uniqKey="Chand M">MA Chand</name></author><author><name sortKey="Brown, Cs" uniqKey="Brown C">CS Brown</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Zaki, Am" uniqKey="Zaki A">AM Zaki</name></author><author><name sortKey="Van Boheemen, S" uniqKey="Van Boheemen S">S van Boheemen</name></author><author><name sortKey="Bestebroer, Tm" 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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></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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