MersV1, PubMed, Curation, bibRecord, 000D09

Structure of the S1 subunit C-terminal domain from bat-derived coronavirus HKU5 spike protein.

Identifieur interne : 000D09 ( PubMed/Curation ); précédent : 000D08; suivant : 000D10

Structure of the S1 subunit C-terminal domain from bat-derived coronavirus HKU5 spike protein.

Auteurs : Xue Han [République populaire de Chine] ; Jianxun Qi [République populaire de Chine] ; Hao Song [République populaire de Chine] ; Qihui Wang [République populaire de Chine] ; Yanfang Zhang [République populaire de Chine] ; Ying Wu [République populaire de Chine] ; Guangwen Lu [République populaire de Chine] ; Kwok-Yung Yuen [République populaire de Chine] ; Yi Shi [République populaire de Chine] ; George F. Gao [République populaire de Chine]

Source :

Virology [ 1096-0341 ] ; 2017.

RBID : pubmed:28432925

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Animals, Chiroptera (genetics), Chiroptera (metabolism), Chiroptera (virology), Coronavirus (chemistry), Coronavirus (classification), Coronavirus (genetics), Coronavirus (metabolism), Coronavirus Infections (genetics), Coronavirus Infections (metabolism), Coronavirus Infections (veterinary), Coronavirus Infections (virology), Dipeptidyl Peptidase 4 (genetics), Dipeptidyl Peptidase 4 (metabolism), Molecular Sequence Data, Protein Conformation, Protein Domains, Receptors, Virus (genetics), Receptors, Virus (metabolism), Sequence Alignment, Spike Glycoprotein, Coronavirus (chemistry), Spike Glycoprotein, Coronavirus (genetics), Spike Glycoprotein, Coronavirus (metabolism).
MESH :
- chemical , chemistry : Spike Glycoprotein, Coronavirus.
- chemical , genetics : Dipeptidyl Peptidase 4, Receptors, Virus, Spike Glycoprotein, Coronavirus.
- chemistry : Coronavirus.
- classification : Coronavirus.
- genetics : Chiroptera, Coronavirus, Coronavirus Infections.
- metabolism : Chiroptera, Coronavirus, Coronavirus Infections, Dipeptidyl Peptidase 4, Receptors, Virus, Spike Glycoprotein, Coronavirus.
- veterinary : Coronavirus Infections.
- virology : Chiroptera, Coronavirus Infections.
- Amino Acid Sequence, Animals, Molecular Sequence Data, Protein Conformation, Protein Domains, Sequence Alignment.

Abstract

Accumulating evidence indicates that MERS-CoV originated from bat coronaviruses (BatCoVs). Previously, we demonstrated that both MERS-CoV and BatCoV HKU4 use CD26 as a receptor, but how the BatCoVs evolved to bind CD26 is an intriguing question. Here, we solved the crystal structure of the S1 subunit C-terminal domain of HKU5 (HKU5-CTD), another BatCoV that is phylogenetically related to MERS-CoV but cannot bind to CD26. We observed that the conserved core subdomain and those of other betacoronaviruses (betaCoVs) have a similar topology of the external subdomain, indicating the same ancestor of lineage C betaCoVs. However, two deletions in two respective loops located in HKU5-CTD result in conformational variations in CD26-binding interface and are responsible for the non-binding of HKU5-CTD to CD26. Combined with sequence variation in the HKU5-CTD receptor binding interface, we propose the necessity for surveilling the mutation in BatCoV HKU5 spike protein in case of bat-to-human interspecies transmission.

DOI: 10.1016/j.virol.2017.04.016
PubMed: 28432925

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<term>Domaines protéiques</term>
<term>Données de séquences moléculaires</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">Accumulating evidence indicates that MERS-CoV originated from bat coronaviruses (BatCoVs). Previously, we demonstrated that both MERS-CoV and BatCoV HKU4 use CD26 as a receptor, but how the BatCoVs evolved to bind CD26 is an intriguing question. Here, we solved the crystal structure of the S1 subunit C-terminal domain of HKU5 (HKU5-CTD), another BatCoV that is phylogenetically related to MERS-CoV but cannot bind to CD26. We observed that the conserved core subdomain and those of other betacoronaviruses (betaCoVs) have a similar topology of the external subdomain, indicating the same ancestor of lineage C betaCoVs. However, two deletions in two respective loops located in HKU5-CTD result in conformational variations in CD26-binding interface and are responsible for the non-binding of HKU5-CTD to CD26. Combined with sequence variation in the HKU5-CTD receptor binding interface, we propose the necessity for surveilling the mutation in BatCoV HKU5 spike protein in case of bat-to-human interspecies transmission.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28432925</PMID>
<DateCompleted><Year>2017</Year>
<Month>07</Month>
<Day>17</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>04</Month>
<Day>07</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1096-0341</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>507</Volume>
<PubDate><Year>2017</Year>
<Month>07</Month>
</PubDate>
</JournalIssue>
<Title>Virology</Title>
<ISOAbbreviation>Virology</ISOAbbreviation>
</Journal>
<ArticleTitle>Structure of the S1 subunit C-terminal domain from bat-derived coronavirus HKU5 spike protein.</ArticleTitle>
<Pagination><MedlinePgn>101-109</MedlinePgn>
</Pagination>
<ELocationID EIdType="pii" ValidYN="Y">S0042-6822(17)30124-1</ELocationID>
<ELocationID EIdType="doi" ValidYN="Y">10.1016/j.virol.2017.04.016</ELocationID>
<Abstract><AbstractText>Accumulating evidence indicates that MERS-CoV originated from bat coronaviruses (BatCoVs). Previously, we demonstrated that both MERS-CoV and BatCoV HKU4 use CD26 as a receptor, but how the BatCoVs evolved to bind CD26 is an intriguing question. Here, we solved the crystal structure of the S1 subunit C-terminal domain of HKU5 (HKU5-CTD), another BatCoV that is phylogenetically related to MERS-CoV but cannot bind to CD26. We observed that the conserved core subdomain and those of other betacoronaviruses (betaCoVs) have a similar topology of the external subdomain, indicating the same ancestor of lineage C betaCoVs. However, two deletions in two respective loops located in HKU5-CTD result in conformational variations in CD26-binding interface and are responsible for the non-binding of HKU5-CTD to CD26. Combined with sequence variation in the HKU5-CTD receptor binding interface, we propose the necessity for surveilling the mutation in BatCoV HKU5 spike protein in case of bat-to-human interspecies transmission.</AbstractText>
<CopyrightInformation>Copyright © 2017 Elsevier Inc. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Han</LastName>
<ForeName>Xue</ForeName>
<Initials>X</Initials>
<AffiliationInfo><Affiliation>CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; University of Chinese Academy of Sciences, Beijing 100049, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Qi</LastName>
<ForeName>Jianxun</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Song</LastName>
<ForeName>Hao</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; Research Network of Immunity and Health (RNIH), Beijing Institutes of Life Science, Chinese Academy of Sciences, Beijing 100101, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wang</LastName>
<ForeName>Qihui</ForeName>
<Initials>Q</Initials>
<AffiliationInfo><Affiliation>CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; Shenzhen Key Laboratory of Pathogen and Immunity, Shenzhen Third People's Hospital, Shenzhen 518112, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhang</LastName>
<ForeName>Yanfang</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; University of Chinese Academy of Sciences, Beijing 100049, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wu</LastName>
<ForeName>Ying</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>Shenzhen Key Laboratory of Pathogen and Immunity, Shenzhen Third People's Hospital, Shenzhen 518112, China; School of Basic Medical Sciences, Wuhan University, Wuhan 430071, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Lu</LastName>
<ForeName>Guangwen</ForeName>
<Initials>G</Initials>
<AffiliationInfo><Affiliation>West China Hospital Emergency Department (WCHED), State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, and Collaborative Innovation Center of Biotherapy, Chengdu, Sichuan 610041, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Yuen</LastName>
<ForeName>Kwok-Yung</ForeName>
<Initials>KY</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory for Emerging Infectious Diseases, The University of Hong Kong, Pokfulam 999077, Hong Kong Special Administration Region; Department of Microbiology, The University of Hong Kong, Pokfulam 999077, Hong Kong Special Administration Region; Collaborative Innovation Center for Diagnosis and Treatment of Infectious Diseases, Zhejiang University, Hangzhou 310003, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Shi</LastName>
<ForeName>Yi</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; University of Chinese Academy of Sciences, Beijing 100049, China; Shenzhen Key Laboratory of Pathogen and Immunity, Shenzhen Third People's Hospital, Shenzhen 518112, China; Center for Influenza Research and Early-warning (CASCIRE), Chinese Academy of Sciences, Beijing 100101, China. Electronic address: shiyi@im.ac.cn.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Gao</LastName>
<ForeName>George F</ForeName>
<Initials>GF</Initials>
<AffiliationInfo><Affiliation>CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; University of Chinese Academy of Sciences, Beijing 100049, China; Research Network of Immunity and Health (RNIH), Beijing Institutes of Life Science, Chinese Academy of Sciences, Beijing 100101, China; Shenzhen Key Laboratory of Pathogen and Immunity, Shenzhen Third People's Hospital, Shenzhen 518112, China; Collaborative Innovation Center for Diagnosis and Treatment of Infectious Diseases, Zhejiang University, Hangzhou 310003, China; Center for Influenza Research and Early-warning (CASCIRE), Chinese Academy of Sciences, Beijing 100101, China; National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention (China CDC), Beijing 102206, China. Electronic address: gaof@im.ac.cn.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2017</Year>
<Month>04</Month>
<Day>19</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Virology</MedlineTA>
<NlmUniqueID>0110674</NlmUniqueID>
<ISSNLinking>0042-6822</ISSNLinking>
</MedlineJournalInfo>
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<NameOfSubstance UI="D011991">Receptors, Virus</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D064370">Spike Glycoprotein, Coronavirus</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="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002685" MajorTopicYN="N">Chiroptera</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000821" MajorTopicYN="Y">virology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017934" MajorTopicYN="N">Coronavirus</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000145" MajorTopicYN="N">classification</QualifierName>
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</MeshHeading>
<MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000072417" MajorTopicYN="N">Protein Domains</DescriptorName>
</MeshHeading>
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<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName>
</MeshHeading>
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<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
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</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">BatCoV HKU5</Keyword>
<Keyword MajorTopicYN="Y">CTD</Keyword>
<Keyword MajorTopicYN="Y">Crystal structure</Keyword>
<Keyword MajorTopicYN="Y">Evolution</Keyword>
<Keyword MajorTopicYN="Y">MERS-CoV</Keyword>
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Structure of the S1 subunit C-terminal domain from bat-derived coronavirus HKU5 spike protein.

Structure of the S1 subunit C-terminal domain from bat-derived coronavirus HKU5 spike protein.

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