Structural Biology of the Arterivirus nsp11 Endoribonucleases.
Identifieur interne : 000A68 ( PubMed/Checkpoint ); précédent : 000A67; suivant : 000A69Structural Biology of the Arterivirus nsp11 Endoribonucleases.
Auteurs : Manfeng Zhang [République populaire de Chine] ; Xiaorong Li [République populaire de Chine] ; Zengqin Deng [République populaire de Chine] ; Zhenhang Chen [République populaire de Chine] ; Yang Liu [République populaire de Chine] ; Yina Gao [République populaire de Chine] ; Wei Wu [République populaire de Chine] ; Zhongzhou Chen [République populaire de Chine]Source :
- Journal of virology [ 1098-5514 ] ; 2017.
Descripteurs français
- KwdFr :
- Alignement de séquences, Coronavirus du syndrome respiratoire du Moyen-Orient (), Coronavirus du syndrome respiratoire du Moyen-Orient (génétique), Coronavirus du syndrome respiratoire du Moyen-Orient (métabolisme), Cristallographie aux rayons X, Domaine catalytique, Domaines protéiques, Endoribonucleases (), Endoribonucleases (génétique), Endoribonucleases (métabolisme), Escherichia coli (génétique), Escherichia coli (métabolisme), Expression des gènes, Modèles moléculaires, Multimérisation de protéines, Mutation, Protéines recombinantes (), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Protéines virales non structurales (), Protéines virales non structurales (génétique), Protéines virales non structurales (métabolisme), Structure secondaire des protéines, Séquence conservée, Séquence d'acides aminés, Virus du SRAS (), Virus du SRAS (génétique), Virus du SRAS (métabolisme), Virus du syndrome respiratoire et reproducteur porcin (), Virus du syndrome respiratoire et reproducteur porcin (enzymologie).
- MESH :
- enzymologie : Virus du syndrome respiratoire et reproducteur porcin.
- génétique : Coronavirus du syndrome respiratoire du Moyen-Orient, Endoribonucleases, Escherichia coli, Protéines recombinantes, Protéines virales non structurales, Virus du SRAS.
- métabolisme : Coronavirus du syndrome respiratoire du Moyen-Orient, Endoribonucleases, Escherichia coli, Protéines recombinantes, Protéines virales non structurales, Virus du SRAS.
- Alignement de séquences, Coronavirus du syndrome respiratoire du Moyen-Orient, Cristallographie aux rayons X, Domaine catalytique, Domaines protéiques, Endoribonucleases, Expression des gènes, Modèles moléculaires, Multimérisation de protéines, Mutation, Protéines recombinantes, Protéines virales non structurales, Structure secondaire des protéines, Séquence conservée, Séquence d'acides aminés, Virus du SRAS, Virus du syndrome respiratoire et reproducteur porcin.
English descriptors
- KwdEn :
- Amino Acid Sequence, Catalytic Domain, Conserved Sequence, Crystallography, X-Ray, Endoribonucleases (chemistry), Endoribonucleases (genetics), Endoribonucleases (metabolism), Equartevirus (chemistry), Equartevirus (enzymology), Escherichia coli (genetics), Escherichia coli (metabolism), Gene Expression, Middle East Respiratory Syndrome Coronavirus (chemistry), Middle East Respiratory Syndrome Coronavirus (genetics), Middle East Respiratory Syndrome Coronavirus (metabolism), Models, Molecular, Mutation, Porcine respiratory and reproductive syndrome virus (chemistry), Porcine respiratory and reproductive syndrome virus (enzymology), Protein Domains, Protein Multimerization, Protein Structure, Secondary, Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), SARS Virus (chemistry), SARS Virus (genetics), SARS Virus (metabolism), Sequence Alignment, Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (metabolism).
- MESH :
- chemical , chemistry : Endoribonucleases, Recombinant Proteins, Viral Nonstructural Proteins.
- chemical , genetics : Endoribonucleases, Recombinant Proteins, Viral Nonstructural Proteins.
- chemical , metabolism : Endoribonucleases, Recombinant Proteins, Viral Nonstructural Proteins.
- chemistry : Equartevirus, Middle East Respiratory Syndrome Coronavirus, Porcine respiratory and reproductive syndrome virus, SARS Virus.
- enzymology : Equartevirus, Porcine respiratory and reproductive syndrome virus.
- genetics : Escherichia coli, Middle East Respiratory Syndrome Coronavirus, SARS Virus.
- metabolism : Escherichia coli, Middle East Respiratory Syndrome Coronavirus, SARS Virus.
- Amino Acid Sequence, Catalytic Domain, Conserved Sequence, Crystallography, X-Ray, Gene Expression, Models, Molecular, Mutation, Protein Domains, Protein Multimerization, Protein Structure, Secondary, Sequence Alignment.
Abstract
Endoribonuclease (NendoU) is unique and conserved as a major genetic marker in nidoviruses that infect vertebrate hosts. Arterivirus nonstructural protein 11 (nsp11) was shown to have NendoU activity and play essential roles in the viral life cycle. Here, we report three crystal structures of porcine reproductive and respiratory syndrome virus (PRRSV) and equine arteritis virus (EAV) nsp11 mutants. The structures of arterivirus nsp11 contain two conserved compact domains: the N-terminal domain (NTD) and C-terminal domain (CTD). The structures of PRRSV and EAV endoribonucleases are similar and conserved in the arterivirus, but they are greatly different from that of severe acute respiratory syndrome (SARS) and Middle East respiratory syndrome (MERS) coronaviruses (CoV), representing important human pathogens in the Nidovirales order. The catalytic center of NendoU activity is located in the CTD, where a positively charged groove is next to the key catalytic residues conserved in nidoviruses. Although the NTD is nearly identical, the catalytic region of the arterivirus nsp11 family proteins is remarkably flexible, and the oligomerization may be concentration dependent. In summary, our structures provide new insight into this key multifunctional NendoU family of proteins and lay a foundation for better understanding of the molecular mechanism and antiviral drug development.
DOI: 10.1128/JVI.01309-16
PubMed: 27795409
Affiliations:
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pubmed:27795409Le document en format XML
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<term>Conserved Sequence</term>
<term>Crystallography, X-Ray</term>
<term>Endoribonucleases (chemistry)</term>
<term>Endoribonucleases (genetics)</term>
<term>Endoribonucleases (metabolism)</term>
<term>Equartevirus (chemistry)</term>
<term>Equartevirus (enzymology)</term>
<term>Escherichia coli (genetics)</term>
<term>Escherichia coli (metabolism)</term>
<term>Gene Expression</term>
<term>Middle East Respiratory Syndrome Coronavirus (chemistry)</term>
<term>Middle East Respiratory Syndrome Coronavirus (genetics)</term>
<term>Middle East Respiratory Syndrome Coronavirus (metabolism)</term>
<term>Models, Molecular</term>
<term>Mutation</term>
<term>Porcine respiratory and reproductive syndrome virus (chemistry)</term>
<term>Porcine respiratory and reproductive syndrome virus (enzymology)</term>
<term>Protein Domains</term>
<term>Protein Multimerization</term>
<term>Protein Structure, Secondary</term>
<term>Recombinant Proteins (chemistry)</term>
<term>Recombinant Proteins (genetics)</term>
<term>Recombinant Proteins (metabolism)</term>
<term>SARS Virus (chemistry)</term>
<term>SARS Virus (genetics)</term>
<term>SARS Virus (metabolism)</term>
<term>Sequence Alignment</term>
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<term>Coronavirus du syndrome respiratoire du Moyen-Orient (métabolisme)</term>
<term>Cristallographie aux rayons X</term>
<term>Domaine catalytique</term>
<term>Domaines protéiques</term>
<term>Endoribonucleases ()</term>
<term>Endoribonucleases (génétique)</term>
<term>Endoribonucleases (métabolisme)</term>
<term>Escherichia coli (génétique)</term>
<term>Escherichia coli (métabolisme)</term>
<term>Expression des gènes</term>
<term>Modèles moléculaires</term>
<term>Multimérisation de protéines</term>
<term>Mutation</term>
<term>Protéines recombinantes ()</term>
<term>Protéines recombinantes (génétique)</term>
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<term>Protéines recombinantes</term>
<term>Protéines virales non structurales</term>
<term>Virus du SRAS</term>
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<term>Middle East Respiratory Syndrome Coronavirus</term>
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<term>Endoribonucleases</term>
<term>Escherichia coli</term>
<term>Protéines recombinantes</term>
<term>Protéines virales non structurales</term>
<term>Virus du SRAS</term>
</keywords>
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<term>Catalytic Domain</term>
<term>Conserved Sequence</term>
<term>Crystallography, X-Ray</term>
<term>Gene Expression</term>
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<term>Mutation</term>
<term>Protein Domains</term>
<term>Protein Multimerization</term>
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<term>Mutation</term>
<term>Protéines recombinantes</term>
<term>Protéines virales non structurales</term>
<term>Structure secondaire des protéines</term>
<term>Séquence conservée</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">Endoribonuclease (NendoU) is unique and conserved as a major genetic marker in nidoviruses that infect vertebrate hosts. Arterivirus nonstructural protein 11 (nsp11) was shown to have NendoU activity and play essential roles in the viral life cycle. Here, we report three crystal structures of porcine reproductive and respiratory syndrome virus (PRRSV) and equine arteritis virus (EAV) nsp11 mutants. The structures of arterivirus nsp11 contain two conserved compact domains: the N-terminal domain (NTD) and C-terminal domain (CTD). The structures of PRRSV and EAV endoribonucleases are similar and conserved in the arterivirus, but they are greatly different from that of severe acute respiratory syndrome (SARS) and Middle East respiratory syndrome (MERS) coronaviruses (CoV), representing important human pathogens in the Nidovirales order. The catalytic center of NendoU activity is located in the CTD, where a positively charged groove is next to the key catalytic residues conserved in nidoviruses. Although the NTD is nearly identical, the catalytic region of the arterivirus nsp11 family proteins is remarkably flexible, and the oligomerization may be concentration dependent. In summary, our structures provide new insight into this key multifunctional NendoU family of proteins and lay a foundation for better understanding of the molecular mechanism and antiviral drug development.</div>
</front>
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<Month>05</Month>
<Day>15</Day>
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<ArticleTitle>Structural Biology of the Arterivirus nsp11 Endoribonucleases.</ArticleTitle>
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<ELocationID EIdType="doi" ValidYN="Y">10.1128/JVI.01309-16</ELocationID>
<Abstract><AbstractText>Endoribonuclease (NendoU) is unique and conserved as a major genetic marker in nidoviruses that infect vertebrate hosts. Arterivirus nonstructural protein 11 (nsp11) was shown to have NendoU activity and play essential roles in the viral life cycle. Here, we report three crystal structures of porcine reproductive and respiratory syndrome virus (PRRSV) and equine arteritis virus (EAV) nsp11 mutants. The structures of arterivirus nsp11 contain two conserved compact domains: the N-terminal domain (NTD) and C-terminal domain (CTD). The structures of PRRSV and EAV endoribonucleases are similar and conserved in the arterivirus, but they are greatly different from that of severe acute respiratory syndrome (SARS) and Middle East respiratory syndrome (MERS) coronaviruses (CoV), representing important human pathogens in the Nidovirales order. The catalytic center of NendoU activity is located in the CTD, where a positively charged groove is next to the key catalytic residues conserved in nidoviruses. Although the NTD is nearly identical, the catalytic region of the arterivirus nsp11 family proteins is remarkably flexible, and the oligomerization may be concentration dependent. In summary, our structures provide new insight into this key multifunctional NendoU family of proteins and lay a foundation for better understanding of the molecular mechanism and antiviral drug development.</AbstractText>
<AbstractText Label="IMPORTANCE" NlmCategory="OBJECTIVE">Porcine reproductive and respiratory syndrome virus (PRRSV) and equine arteritis virus are two major members of the arterivirus family. PRRSV, a leading swine pathogen, causes reproductive failure in breeding stock and respiratory tract illness in young pigs. Due to the lack of a suitable vaccine or effective drug treatment and the quick spread of these viruses, infected animals either die quickly or must be culled. PRRSV costs the swine industry around $644 million annually in the United States and almost €1.5 billion in Europe every year. To find a way to combat these viruses, we focused on the essential viral nonstructural protein 11 (nsp11). nsp11 is associated with multiple functions, such as RNA processing and suppression of the infected host innate immunity system. The three structures solved in this study provide new insight into the molecular mechanisms of this crucial protein family and will benefit the development of new treatments against these deadly viruses.</AbstractText>
<CopyrightInformation>Copyright © 2016 American Society for Microbiology.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zhang</LastName>
<ForeName>Manfeng</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Beijing Advanced Innovation Center for Food Nutrition and Human Health, China Agricultural University, Beijing, China.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>State Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Li</LastName>
<ForeName>Xiaorong</ForeName>
<Initials>X</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Deng</LastName>
<ForeName>Zengqin</ForeName>
<Initials>Z</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Chen</LastName>
<ForeName>Zhenhang</ForeName>
<Initials>Z</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Liu</LastName>
<ForeName>Yang</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Gao</LastName>
<ForeName>Yina</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wu</LastName>
<ForeName>Wei</ForeName>
<Initials>W</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Chen</LastName>
<ForeName>Zhongzhou</ForeName>
<Initials>Z</Initials>
<Identifier Source="ORCID">http://orcid.org/0000-0003-1319-9664</Identifier>
<AffiliationInfo><Affiliation>Beijing Advanced Innovation Center for Food Nutrition and Human Health, China Agricultural University, Beijing, China chenzhongzhou@cau.edu.cn.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>State Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing, China.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2016</Year>
<Month>12</Month>
<Day>16</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="D011994">Recombinant Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D017361">Viral Nonstructural Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.1.-</RegistryNumber>
<NameOfSubstance UI="D004722">Endoribonucleases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.1.-</RegistryNumber>
<NameOfSubstance UI="C000657925">nidoviral uridylate-specific endoribonuclease</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017124" MajorTopicYN="N">Conserved Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004722" MajorTopicYN="N">Endoribonucleases</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007240" MajorTopicYN="N">Equartevirus</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015870" MajorTopicYN="N">Gene Expression</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D065207" MajorTopicYN="N">Middle East Respiratory Syndrome Coronavirus</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D019316" MajorTopicYN="N">Porcine respiratory and reproductive syndrome virus</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000072417" MajorTopicYN="N">Protein Domains</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<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>
<MeshHeading><DescriptorName UI="D017361" MajorTopicYN="N">Viral Nonstructural Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">EAV</Keyword>
<Keyword MajorTopicYN="Y">NendoU</Keyword>
<Keyword MajorTopicYN="Y">PRRSV</Keyword>
<Keyword MajorTopicYN="Y">arterivirus</Keyword>
<Keyword MajorTopicYN="Y">crystal structures</Keyword>
<Keyword MajorTopicYN="Y">flexibility</Keyword>
<Keyword MajorTopicYN="Y">mutagenesis</Keyword>
<Keyword MajorTopicYN="Y">nsp11</Keyword>
</KeywordList>
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<Month>10</Month>
<Day>01</Day>
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<affiliations><list><country><li>République populaire de Chine</li>
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<name sortKey="Chen, Zhenhang" sort="Chen, Zhenhang" uniqKey="Chen Z" first="Zhenhang" last="Chen">Zhenhang Chen</name>
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