Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4.
Identifieur interne : 001098 ( PubMed/Checkpoint ); précédent : 001097; suivant : 001099Structure 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:
Links toward previous steps (curation, corpus...)
Links to Exploration step
pubmed:23835475Le document en format XML
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<term>Protein Structure, Tertiary</term>
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<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>
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<Abstract><AbstractText>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.</AbstractText>
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<ReferenceList><Reference><Citation>Nature. 1992 Jun 4;357(6377):420-2</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1350662</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2003 Nov 27;426(6965):450-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14647384</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 1994 Sep 1;50(Pt 5):760-3</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15299374</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 2005 Sep 16;309(5742):1864-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16166518</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Microbiol Mol Biol Rev. 2005 Dec;69(4):635-64</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16339739</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Adv Virus Res. 2006;66:193-292</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16877062</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2006 Sep;62(Pt 9):1002-11</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16929101</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2008 Jan;64(Pt 1):49-60</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18094467</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Rev Microbiol. 2009 Mar;7(3):226-36</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19198616</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19461840</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2009 Nov 24;106(47):19970-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19901337</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2011 Apr 22;286(16):14531-41</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21325278</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Infect. 2012 Dec;65(6):477-89</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23072791</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>N Engl J Med. 2012 Nov 8;367(19):1814-20</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23075143</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Euro Surveill. 2012 Oct 04;17(40):20290</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23078800</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>MBio. 2012 Nov 20;3(6):null</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23170002</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Infect. 2013 May;66(5):464-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23266463</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2013 Mar 14;495(7440):176-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23486053</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2013 Mar 14;495(7440):251-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23486063</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Infect. 2013 Aug;67(2):156-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23603488</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2013 Jul;87(14):7790-2</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23678167</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>N Engl J Med. 2013 Jun 27;368(26):2487-94</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23718156</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Emerg Microbes Infect. 2012 Nov;1(11):e35</Citation>
<ArticleIdList><ArticleId IdType="pubmed">26038405</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Enzymol. 1997;276:307-26</Citation>
<ArticleIdList><ArticleId IdType="pubmed">27754618</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>République populaire de Chine</li>
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<settlement><li>Pékin</li>
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<name sortKey="Cui, Ye" sort="Cui, Ye" uniqKey="Cui Y" first="Ye" last="Cui">Ye Cui</name>
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