Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus.
Identifieur interne : 001C37 ( PubMed/Corpus ); précédent : 001C36; suivant : 001C38Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus.
Auteurs : Yaoqing Chen ; Kanagalaghatta R. Rajashankar ; Yang Yang ; Sudhakar S. Agnihothram ; Chang Liu ; Yi-Lun Lin ; Ralph S. Baric ; Fang LiSource :
- Journal of virology [ 1098-5514 ] ; 2013.
English descriptors
- KwdEn :
- Amino Acid Sequence, Coronavirus (physiology), Crystallography, X-Ray, Dipeptidyl Peptidase 4 (metabolism), Host-Pathogen Interactions, Humans, Leukemia Virus, Murine (genetics), Middle East, Molecular Sequence Data, Protein Conformation, Sequence Homology, Amino Acid, Syndrome, Viral Proteins (chemistry), Viral Proteins (metabolism).
- MESH :
- chemical , chemistry : Viral Proteins.
- chemical , metabolism : Dipeptidyl Peptidase 4, Viral Proteins.
- geographic : Middle East.
- genetics : Leukemia Virus, Murine.
- physiology : Coronavirus.
- Amino Acid Sequence, Crystallography, X-Ray, Host-Pathogen Interactions, Humans, Molecular Sequence Data, Protein Conformation, Sequence Homology, Amino Acid, Syndrome.
Abstract
The newly emerged Middle East respiratory syndrome coronavirus (MERS-CoV) has infected at least 77 people, with a fatality rate of more than 50%. Alarmingly, the virus demonstrates the capability of human-to-human transmission, raising the possibility of global spread and endangering world health and economy. Here we have identified the receptor-binding domain (RBD) from the MERS-CoV spike protein and determined its crystal structure. This study also presents a structural comparison of MERS-CoV RBD with other coronavirus RBDs, successfully positioning MERS-CoV on the landscape of coronavirus evolution and providing insights into receptor binding by MERS-CoV. Furthermore, we found that MERS-CoV RBD functions as an effective entry inhibitor of MERS-CoV. The identified MERS-CoV RBD may also serve as a potential candidate for MERS-CoV subunit vaccines. Overall, this study enhances our understanding of the evolution of coronavirus RBDs, provides insights into receptor recognition by MERS-CoV, and may help control the transmission of MERS-CoV in humans.
DOI: 10.1128/JVI.01756-13
PubMed: 23903833
Links to Exploration step
pubmed:23903833Le document en format XML
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Agnihothram</name></author><author><name sortKey="Liu, Chang" sort="Liu, Chang" uniqKey="Liu C" first="Chang" last="Liu">Chang Liu</name></author><author><name sortKey="Lin, Yi Lun" sort="Lin, Yi Lun" uniqKey="Lin Y" first="Yi-Lun" last="Lin">Yi-Lun Lin</name></author><author><name sortKey="Baric, Ralph S" sort="Baric, Ralph S" uniqKey="Baric R" first="Ralph S" last="Baric">Ralph S. Baric</name></author><author><name sortKey="Li, Fang" sort="Li, Fang" uniqKey="Li F" first="Fang" last="Li">Fang Li</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2013">2013</date><idno type="RBID">pubmed:23903833</idno><idno type="pmid">23903833</idno><idno type="doi">10.1128/JVI.01756-13</idno><idno type="wicri:Area/PubMed/Corpus">001C37</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001C37</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus.</title><author><name sortKey="Chen, Yaoqing" sort="Chen, Yaoqing" uniqKey="Chen Y" first="Yaoqing" last="Chen">Yaoqing Chen</name><affiliation><nlm:affiliation>Department of Pharmacology, University of Minnesota Medical School, Minneapolis, Minnesota, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Rajashankar, Kanagalaghatta R" sort="Rajashankar, Kanagalaghatta R" uniqKey="Rajashankar K" first="Kanagalaghatta R" last="Rajashankar">Kanagalaghatta R. Rajashankar</name></author><author><name sortKey="Yang, Yang" sort="Yang, Yang" uniqKey="Yang Y" first="Yang" last="Yang">Yang Yang</name></author><author><name sortKey="Agnihothram, Sudhakar S" sort="Agnihothram, Sudhakar S" uniqKey="Agnihothram S" first="Sudhakar S" last="Agnihothram">Sudhakar S. Agnihothram</name></author><author><name sortKey="Liu, Chang" sort="Liu, Chang" uniqKey="Liu C" first="Chang" last="Liu">Chang Liu</name></author><author><name sortKey="Lin, Yi Lun" sort="Lin, Yi Lun" uniqKey="Lin Y" first="Yi-Lun" last="Lin">Yi-Lun Lin</name></author><author><name sortKey="Baric, Ralph S" sort="Baric, Ralph S" uniqKey="Baric R" first="Ralph S" last="Baric">Ralph S. Baric</name></author><author><name sortKey="Li, Fang" sort="Li, Fang" uniqKey="Li F" first="Fang" last="Li">Fang Li</name></author></analytic><series><title level="j">Journal of virology</title><idno type="eISSN">1098-5514</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 Sequence</term><term>Coronavirus (physiology)</term><term>Crystallography, X-Ray</term><term>Dipeptidyl Peptidase 4 (metabolism)</term><term>Host-Pathogen Interactions</term><term>Humans</term><term>Leukemia Virus, Murine (genetics)</term><term>Middle East</term><term>Molecular Sequence Data</term><term>Protein Conformation</term><term>Sequence Homology, Amino Acid</term><term>Syndrome</term><term>Viral Proteins (chemistry)</term><term>Viral Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Dipeptidyl Peptidase 4</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="geographic" xml:lang="en"><term>Middle East</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Leukemia Virus, Murine</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Coronavirus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Crystallography, X-Ray</term><term>Host-Pathogen Interactions</term><term>Humans</term><term>Molecular Sequence Data</term><term>Protein Conformation</term><term>Sequence Homology, Amino Acid</term><term>Syndrome</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The newly emerged Middle East respiratory syndrome coronavirus (MERS-CoV) has infected at least 77 people, with a fatality rate of more than 50%. Alarmingly, the virus demonstrates the capability of human-to-human transmission, raising the possibility of global spread and endangering world health and economy. Here we have identified the receptor-binding domain (RBD) from the MERS-CoV spike protein and determined its crystal structure. This study also presents a structural comparison of MERS-CoV RBD with other coronavirus RBDs, successfully positioning MERS-CoV on the landscape of coronavirus evolution and providing insights into receptor binding by MERS-CoV. Furthermore, we found that MERS-CoV RBD functions as an effective entry inhibitor of MERS-CoV. The identified MERS-CoV RBD may also serve as a potential candidate for MERS-CoV subunit vaccines. Overall, this study enhances our understanding of the evolution of coronavirus RBDs, provides insights into receptor recognition by MERS-CoV, and may help control the transmission of MERS-CoV in humans. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23903833</PMID><DateCompleted><Year>2013</Year><Month>12</Month><Day>27</Day></DateCompleted><DateRevised><Year>2019</Year><Month>01</Month><Day>08</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1098-5514</ISSN><JournalIssue CitedMedium="Internet"><Volume>87</Volume><Issue>19</Issue><PubDate><Year>2013</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Journal of virology</Title><ISOAbbreviation>J. Virol.</ISOAbbreviation></Journal><ArticleTitle>Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus.</ArticleTitle><Pagination><MedlinePgn>10777-83</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1128/JVI.01756-13</ELocationID><Abstract><AbstractText>The newly emerged Middle East respiratory syndrome coronavirus (MERS-CoV) has infected at least 77 people, with a fatality rate of more than 50%. Alarmingly, the virus demonstrates the capability of human-to-human transmission, raising the possibility of global spread and endangering world health and economy. Here we have identified the receptor-binding domain (RBD) from the MERS-CoV spike protein and determined its crystal structure. This study also presents a structural comparison of MERS-CoV RBD with other coronavirus RBDs, successfully positioning MERS-CoV on the landscape of coronavirus evolution and providing insights into receptor binding by MERS-CoV. Furthermore, we found that MERS-CoV RBD functions as an effective entry inhibitor of MERS-CoV. The identified MERS-CoV RBD may also serve as a potential candidate for MERS-CoV subunit vaccines. Overall, this study enhances our understanding of the evolution of coronavirus RBDs, provides insights into receptor recognition by MERS-CoV, and may help control the transmission of MERS-CoV in humans. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Yaoqing</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Pharmacology, University of Minnesota Medical School, Minneapolis, Minnesota, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rajashankar</LastName><ForeName>Kanagalaghatta R</ForeName><Initials>KR</Initials></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Yang</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Agnihothram</LastName><ForeName>Sudhakar S</ForeName><Initials>SS</Initials></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Chang</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Lin</LastName><ForeName>Yi-Lun</ForeName><Initials>YL</Initials></Author><Author ValidYN="Y"><LastName>Baric</LastName><ForeName>Ralph S</ForeName><Initials>RS</Initials></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Fang</ForeName><Initials>F</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>1U19AI100625</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 AI089728</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 AI085524</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>P41 GM103403</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01AI089728</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01AI085524</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>8P41GM103403-10</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>U19 AI100625</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>07</Month><Day>31</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Virol</MedlineTA><NlmUniqueID>0113724</NlmUniqueID><ISSNLinking>0022-538X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014764">Viral Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.14.5</RegistryNumber><NameOfSubstance UI="C042807">DPP4 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.14.5</RegistryNumber><NameOfSubstance UI="D018819">Dipeptidyl Peptidase 4</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017934" MajorTopicYN="N">Coronavirus</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName 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