Structural basis for dimerization and RNA binding of avian infectious bronchitis virus nsp9.
Identifieur interne : 000B47 ( PubMed/Curation ); précédent : 000B46; suivant : 000B48Structural basis for dimerization and RNA binding of avian infectious bronchitis virus nsp9.
Auteurs : Tingting Hu [République populaire de Chine] ; Cheng Chen [République populaire de Chine] ; Huiyan Li [République populaire de Chine] ; Yanshu Dou [République populaire de Chine] ; Ming Zhou [République populaire de Chine] ; Deren Lu [République populaire de Chine] ; Qi Zong [République populaire de Chine] ; Yulei Li [République populaire de Chine] ; Cheng Yang [République populaire de Chine] ; Zhihui Zhong [République populaire de Chine] ; Namit Singh [États-Unis] ; Honggang Hu [République populaire de Chine] ; Rundong Zhang [République populaire de Chine] ; Haitao Yang [République populaire de Chine] ; Dan Su [République populaire de Chine]Source :
- Protein science : a publication of the Protein Society [ 1469-896X ] ; 2017.
Descripteurs français
- KwdFr :
- ARN viral (), ARN viral (métabolisme), Multimérisation de protéines, Protéines de liaison à l'ARN (), Protéines de liaison à l'ARN (métabolisme), Protéines virales (), Protéines virales (métabolisme), Relation structure-activité, Virus de la bronchite infectieuse (), Virus de la bronchite infectieuse (métabolisme).
- MESH :
English descriptors
- KwdEn :
- Infectious bronchitis virus (chemistry), Infectious bronchitis virus (metabolism), Protein Multimerization, RNA, Viral (chemistry), RNA, Viral (metabolism), RNA-Binding Proteins (chemistry), RNA-Binding Proteins (metabolism), Structure-Activity Relationship, Viral Proteins (chemistry), Viral Proteins (metabolism).
- MESH :
- chemical , chemistry : RNA, Viral, RNA-Binding Proteins, Viral Proteins.
- chemistry : Infectious bronchitis virus.
- metabolism : Infectious bronchitis virus, RNA, Viral, RNA-Binding Proteins, Viral Proteins.
- Protein Multimerization, Structure-Activity Relationship.
Abstract
The potential for infection by coronaviruses (CoVs) has become a serious concern with the recent emergence of Middle East respiratory syndrome and severe acute respiratory syndrome (SARS) in the human population. CoVs encode two large polyproteins, which are then processed into 15-16 nonstructural proteins (nsps) that make significant contributions to viral replication and transcription by assembling the RNA replicase complex. Among them, nsp9 plays an essential role in viral replication by forming a homodimer that binds single-stranded RNA. Thus, disrupting nsp9 dimerization is a potential anti-CoV therapy. However, different nsp9 dimer forms have been reported for alpha- and beta-CoVs, and no structural information is available for gamma-CoVs. Here we determined the crystal structure of nsp9 from the avian infectious bronchitis virus (IBV), a representative gamma-CoV that affects the economy of the poultry industry because it can infect domestic fowl. IBV nsp9 forms a homodimer via interactions across a hydrophobic interface, which consists of two parallel alpha helices near the carboxy terminus of the protein. The IBV nsp9 dimer resembles that of SARS-CoV nsp9, indicating that this type of dimerization is conserved among all CoVs. This makes disruption of the dimeric interface an excellent strategy for developing anti-CoV therapies. To facilitate this effort, we characterized the roles of six conserved residues on this interface using site-directed mutagenesis and a multitude of biochemical and biophysical methods. We found that three residues are critical for nsp9 dimerization and its abitlity to bind RNA.
DOI: 10.1002/pro.3150
PubMed: 28257598
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<author><name sortKey="Zong, Qi" sort="Zong, Qi" uniqKey="Zong Q" first="Qi" last="Zong">Qi Zong</name>
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<author><name sortKey="Yang, Cheng" sort="Yang, Cheng" uniqKey="Yang C" first="Cheng" last="Yang">Cheng Yang</name>
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<author><name sortKey="Zhong, Zhihui" sort="Zhong, Zhihui" uniqKey="Zhong Z" first="Zhihui" last="Zhong">Zhihui Zhong</name>
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<author><name sortKey="Singh, Namit" sort="Singh, Namit" uniqKey="Singh N" first="Namit" last="Singh">Namit Singh</name>
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<author><name sortKey="Hu, Honggang" sort="Hu, Honggang" uniqKey="Hu H" first="Honggang" last="Hu">Honggang Hu</name>
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<author><name sortKey="Zhang, Rundong" sort="Zhang, Rundong" uniqKey="Zhang R" first="Rundong" last="Zhang">Rundong Zhang</name>
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<author><name sortKey="Yang, Haitao" sort="Yang, Haitao" uniqKey="Yang H" first="Haitao" last="Yang">Haitao Yang</name>
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<author><name sortKey="Su, Dan" sort="Su, Dan" uniqKey="Su D" first="Dan" last="Su">Dan Su</name>
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<term>RNA, Viral (metabolism)</term>
<term>RNA-Binding Proteins (chemistry)</term>
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<front><div type="abstract" xml:lang="en">The potential for infection by coronaviruses (CoVs) has become a serious concern with the recent emergence of Middle East respiratory syndrome and severe acute respiratory syndrome (SARS) in the human population. CoVs encode two large polyproteins, which are then processed into 15-16 nonstructural proteins (nsps) that make significant contributions to viral replication and transcription by assembling the RNA replicase complex. Among them, nsp9 plays an essential role in viral replication by forming a homodimer that binds single-stranded RNA. Thus, disrupting nsp9 dimerization is a potential anti-CoV therapy. However, different nsp9 dimer forms have been reported for alpha- and beta-CoVs, and no structural information is available for gamma-CoVs. Here we determined the crystal structure of nsp9 from the avian infectious bronchitis virus (IBV), a representative gamma-CoV that affects the economy of the poultry industry because it can infect domestic fowl. IBV nsp9 forms a homodimer via interactions across a hydrophobic interface, which consists of two parallel alpha helices near the carboxy terminus of the protein. The IBV nsp9 dimer resembles that of SARS-CoV nsp9, indicating that this type of dimerization is conserved among all CoVs. This makes disruption of the dimeric interface an excellent strategy for developing anti-CoV therapies. To facilitate this effort, we characterized the roles of six conserved residues on this interface using site-directed mutagenesis and a multitude of biochemical and biophysical methods. We found that three residues are critical for nsp9 dimerization and its abitlity to bind RNA.</div>
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<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28257598</PMID>
<DateCompleted><Year>2017</Year>
<Month>07</Month>
<Day>17</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1469-896X</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>26</Volume>
<Issue>5</Issue>
<PubDate><Year>2017</Year>
<Month>05</Month>
</PubDate>
</JournalIssue>
<Title>Protein science : a publication of the Protein Society</Title>
<ISOAbbreviation>Protein Sci.</ISOAbbreviation>
</Journal>
<ArticleTitle>Structural basis for dimerization and RNA binding of avian infectious bronchitis virus nsp9.</ArticleTitle>
<Pagination><MedlinePgn>1037-1048</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1002/pro.3150</ELocationID>
<Abstract><AbstractText>The potential for infection by coronaviruses (CoVs) has become a serious concern with the recent emergence of Middle East respiratory syndrome and severe acute respiratory syndrome (SARS) in the human population. CoVs encode two large polyproteins, which are then processed into 15-16 nonstructural proteins (nsps) that make significant contributions to viral replication and transcription by assembling the RNA replicase complex. Among them, nsp9 plays an essential role in viral replication by forming a homodimer that binds single-stranded RNA. Thus, disrupting nsp9 dimerization is a potential anti-CoV therapy. However, different nsp9 dimer forms have been reported for alpha- and beta-CoVs, and no structural information is available for gamma-CoVs. Here we determined the crystal structure of nsp9 from the avian infectious bronchitis virus (IBV), a representative gamma-CoV that affects the economy of the poultry industry because it can infect domestic fowl. IBV nsp9 forms a homodimer via interactions across a hydrophobic interface, which consists of two parallel alpha helices near the carboxy terminus of the protein. The IBV nsp9 dimer resembles that of SARS-CoV nsp9, indicating that this type of dimerization is conserved among all CoVs. This makes disruption of the dimeric interface an excellent strategy for developing anti-CoV therapies. To facilitate this effort, we characterized the roles of six conserved residues on this interface using site-directed mutagenesis and a multitude of biochemical and biophysical methods. We found that three residues are critical for nsp9 dimerization and its abitlity to bind RNA.</AbstractText>
<CopyrightInformation>© 2017 The Protein Society.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hu</LastName>
<ForeName>Tingting</ForeName>
<Initials>T</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, and Collaborative Innovation Center for Biotherapy, Chengdu, 610041, P.R. China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Chen</LastName>
<ForeName>Cheng</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>School of Life Sciences, Tianjin University, Tianjin, 300072, P.R. China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Li</LastName>
<ForeName>Huiyan</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, and Collaborative Innovation Center for Biotherapy, Chengdu, 610041, P.R. China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Dou</LastName>
<ForeName>Yanshu</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, and Collaborative Innovation Center for Biotherapy, Chengdu, 610041, P.R. China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhou</LastName>
<ForeName>Ming</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, and Collaborative Innovation Center for Biotherapy, Chengdu, 610041, P.R. China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Lu</LastName>
<ForeName>Deren</ForeName>
<Initials>D</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, and Collaborative Innovation Center for Biotherapy, Chengdu, 610041, P.R. China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zong</LastName>
<ForeName>Qi</ForeName>
<Initials>Q</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, and Collaborative Innovation Center for Biotherapy, Chengdu, 610041, P.R. China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Li</LastName>
<ForeName>Yulei</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>Department of Organic Chemistry, School of Pharmacy, Second Military Medical University, Shanghai, 200433, P.R. China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Yang</LastName>
<ForeName>Cheng</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>College of Chemistry, Sichuan University, Chengdu, 610041, P.R. China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhong</LastName>
<ForeName>Zhihui</ForeName>
<Initials>Z</Initials>
<AffiliationInfo><Affiliation>Laboratory of Non-human Primate Disease Modeling Research, West China Hospital, Sichuan University, Chengdu, 610041, P.R. China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Singh</LastName>
<ForeName>Namit</ForeName>
<Initials>N</Initials>
<AffiliationInfo><Affiliation>Ludwig Institute for Cancer Research, University of California, La Jolla, San Diego, California, 92093, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Hu</LastName>
<ForeName>Honggang</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>Department of Organic Chemistry, School of Pharmacy, Second Military Medical University, Shanghai, 200433, P.R. China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhang</LastName>
<ForeName>Rundong</ForeName>
<Initials>R</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, and Collaborative Innovation Center for Biotherapy, Chengdu, 610041, P.R. China.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Ophthalmology, West China Hospital, Sichuan University, Chengdu, 610041, P.R. China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Yang</LastName>
<ForeName>Haitao</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>School of Life Sciences, Tianjin University, Tianjin, 300072, P.R. China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Su</LastName>
<ForeName>Dan</ForeName>
<Initials>D</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, and Collaborative Innovation Center for Biotherapy, Chengdu, 610041, P.R. China.</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>20</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Protein Sci</MedlineTA>
<NlmUniqueID>9211750</NlmUniqueID>
<ISSNLinking>0961-8368</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D012367">RNA, Viral</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D016601">RNA-Binding Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D014764">Viral Proteins</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D001351" MajorTopicYN="N">Infectious bronchitis virus</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D055503" MajorTopicYN="Y">Protein Multimerization</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012367" MajorTopicYN="N">RNA, Viral</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016601" MajorTopicYN="N">RNA-Binding Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013329" MajorTopicYN="N">Structure-Activity Relationship</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014764" MajorTopicYN="N">Viral Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Nsp9</Keyword>
<Keyword MajorTopicYN="Y">coronaviruses</Keyword>
<Keyword MajorTopicYN="Y">dimerization</Keyword>
<Keyword MajorTopicYN="Y">infectious bronchitis virus</Keyword>
<Keyword MajorTopicYN="Y">nonstructural proteins</Keyword>
</KeywordList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year>
<Month>12</Month>
<Day>01</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="revised"><Year>2017</Year>
<Month>02</Month>
<Day>28</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2017</Year>
<Month>02</Month>
<Day>28</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2017</Year>
<Month>3</Month>
<Day>4</Day>
<Hour>6</Hour>
<Minute>0</Minute>
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<PubMedPubDate PubStatus="medline"><Year>2017</Year>
<Month>7</Month>
<Day>18</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2017</Year>
<Month>3</Month>
<Day>4</Day>
<Hour>6</Hour>
<Minute>0</Minute>
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