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Structural Biology of the Arterivirus nsp11 Endoribonucleases.

Identifieur interne : 000F16 ( PubMed/Curation ); précédent : 000F15; suivant : 000F17

Structural 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.

RBID : pubmed:27795409

Descripteurs français

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

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<term>Recombinant Proteins (metabolism)</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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<DateCompleted><Year>2017</Year>
<Month>05</Month>
<Day>15</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>03</Month>
<Day>26</Day>
</DateRevised>
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<Issue>1</Issue>
<PubDate><Year>2017</Year>
<Month>Jan</Month>
<Day>01</Day>
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</JournalIssue>
<Title>Journal of virology</Title>
<ISOAbbreviation>J. Virol.</ISOAbbreviation>
</Journal>
<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>
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<Author ValidYN="Y"><LastName>Deng</LastName>
<ForeName>Zengqin</ForeName>
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<AffiliationInfo><Affiliation>State Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing, China.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Chen</LastName>
<ForeName>Zhenhang</ForeName>
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</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Liu</LastName>
<ForeName>Yang</ForeName>
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<ForeName>Yina</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing, China.</Affiliation>
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<ForeName>Wei</ForeName>
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<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>
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Structural Biology of the Arterivirus nsp11 Endoribonucleases.

Structural Biology of the Arterivirus nsp11 Endoribonucleases.

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