Insight into the evolution of nidovirus endoribonuclease based on the finding that nsp15 from porcine Deltacoronavirus functions as a dimer.
Identifieur interne : 000996 ( PubMed/Checkpoint ); précédent : 000995; suivant : 000997Insight into the evolution of nidovirus endoribonuclease based on the finding that nsp15 from porcine Deltacoronavirus functions as a dimer.
Auteurs : Anjun Zheng ; Yuejun Shi ; Zhou Shen ; Gang Wang ; Jiale Shi ; Qiqi Xiong ; Liurong Fang ; Shaobo Xiao ; Zhen F. Fu [États-Unis] ; Guiqing Peng [République populaire de Chine]Source :
- The Journal of biological chemistry [ 1083-351X ] ; 2018.
Descripteurs français
- KwdFr :
- Alignement de séquences, Arterivirus (), Arterivirus (génétique), Arterivirus (métabolisme), Clonage moléculaire, Coronavirus (), Coronavirus (génétique), Coronavirus (métabolisme), Cristallographie aux rayons X, Endoribonucleases (), Endoribonucleases (génétique), Endoribonucleases (métabolisme), Escherichia coli (génétique), Escherichia coli (métabolisme), Expression des gènes, Liaison aux protéines, Modèles moléculaires, Motifs et domaines d'intéraction protéique, Multimérisation de protéines, Nidovirales (), Nidovirales (génétique), Nidovirales (métabolisme), Protéines recombinantes (), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Protéines virales non structurales (), Protéines virales non structurales (génétique), Protéines virales non structurales (métabolisme), Réplication virale (génétique), Similitude de séquences d'acides aminés, Sites de fixation, Sous-unités de protéines (), Sous-unités de protéines (génétique), Sous-unités de protéines (métabolisme), Structure en brin bêta, Structure en hélice alpha, Séquence d'acides aminés, Vecteurs génétiques (), Vecteurs génétiques (métabolisme), Virus du SRAS (), Virus du SRAS (génétique), Virus du SRAS (métabolisme), Évolution moléculaire.
- MESH :
- génétique : Arterivirus, Coronavirus, Endoribonucleases, Escherichia coli, Nidovirales, Protéines recombinantes, Protéines virales non structurales, Réplication virale, Sous-unités de protéines, Virus du SRAS.
- métabolisme : Arterivirus, Coronavirus, Endoribonucleases, Escherichia coli, Nidovirales, Protéines recombinantes, Protéines virales non structurales, Sous-unités de protéines, Vecteurs génétiques, Virus du SRAS.
- Alignement de séquences, Arterivirus, Clonage moléculaire, Coronavirus, Cristallographie aux rayons X, Endoribonucleases, Expression des gènes, Liaison aux protéines, Modèles moléculaires, Motifs et domaines d'intéraction protéique, Multimérisation de protéines, Nidovirales, Protéines recombinantes, Protéines virales non structurales, Similitude de séquences d'acides aminés, Sites de fixation, Sous-unités de protéines, Structure en brin bêta, Structure en hélice alpha, Séquence d'acides aminés, Vecteurs génétiques, Virus du SRAS, Évolution moléculaire.
English descriptors
- KwdEn :
- Amino Acid Sequence, Arterivirus (chemistry), Arterivirus (classification), Arterivirus (genetics), Arterivirus (metabolism), Binding Sites, Cloning, Molecular, Coronavirus (chemistry), Coronavirus (classification), Coronavirus (genetics), Coronavirus (metabolism), Crystallography, X-Ray, Endoribonucleases (chemistry), Endoribonucleases (genetics), Endoribonucleases (metabolism), Escherichia coli (genetics), Escherichia coli (metabolism), Evolution, Molecular, Gene Expression, Genetic Vectors (chemistry), Genetic Vectors (metabolism), Models, Molecular, Nidovirales (chemistry), Nidovirales (classification), Nidovirales (genetics), Nidovirales (metabolism), Protein Binding, Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Protein Interaction Domains and Motifs, Protein Multimerization, Protein Subunits (chemistry), Protein Subunits (genetics), Protein Subunits (metabolism), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), SARS Virus (chemistry), SARS Virus (classification), SARS Virus (genetics), SARS Virus (metabolism), Sequence Alignment, Sequence Homology, Amino Acid, Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (metabolism), Virus Replication (genetics).
- MESH :
- chemical , chemistry : Endoribonucleases, Protein Subunits, Recombinant Proteins, Viral Nonstructural Proteins.
- chemistry : Arterivirus, Coronavirus, Genetic Vectors, Nidovirales, SARS Virus.
- classification : Arterivirus, Coronavirus, Nidovirales, SARS Virus.
- genetics : Arterivirus, Coronavirus, Endoribonucleases, Escherichia coli, Nidovirales, Protein Subunits, Recombinant Proteins, SARS Virus, Viral Nonstructural Proteins, Virus Replication.
- metabolism : Arterivirus, Coronavirus, Endoribonucleases, Escherichia coli, Genetic Vectors, Nidovirales, Protein Subunits, Recombinant Proteins, SARS Virus, Viral Nonstructural Proteins.
- Amino Acid Sequence, Binding Sites, Cloning, Molecular, Crystallography, X-Ray, Evolution, Molecular, Gene Expression, Models, Molecular, Protein Binding, Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Protein Interaction Domains and Motifs, Protein Multimerization, Sequence Alignment, Sequence Homology, Amino Acid.
Abstract
Nidovirus endoribonucleases (NendoUs) include nonstructural protein 15 (nsp15) from coronaviruses and nsp11 from arteriviruses, both of which have been reported to participate in the viral replication process and in the evasion of the host immune system. Results from a previous study of coronaviruses SARS-CoV, HCoV-229E, and MHV nsp15 indicate that it mainly forms a functional hexamer, whereas nsp11 from the arterivirus PRRSV is a dimer. Here, we found that porcine Deltacoronavirus (PDCoV) nsp15 primarily exists as dimers and monomers in vitro Biological experiments reveal that a PDCoV nsp15 mutant lacking the first 27 amino acids of the N-terminal domain (Asn-1-Asn-27) forms more monomers and displays decreased enzymatic activity, indicating that this region is important for its dimerization. Moreover, multiple sequence alignments and three-dimensional structural analysis indicated that the C-terminal region (His-251-Val-261) of PDCoV nsp15 is 10 amino acids shorter and forms a shorter loop than that formed by the equivalent sequence (Gln-259-Phe-279) of SARS-CoV nsp15. This result may explain why PDCoV nsp15 failed to form hexamers. We speculate that NendoUs may have originated from XendoU endoribonucleases (XendoUs) forming monomers in eukaryotic cells, that NendoU from arterivirus gained the ability to form dimers, and that the coronavirus variants then evolved the capacity to assemble into hexamers. We further propose that PDCoV nsp15 may be an intermediate in this evolutionary process. Our findings provide a theoretical basis for improving our understanding of NendoU evolution and offer useful clues for designing drugs and vaccines against nidoviruses.
DOI: 10.1074/jbc.RA118.003756
PubMed: 29887523
Affiliations:
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pubmed:29887523Le document en format XML
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<term>Arterivirus (chemistry)</term>
<term>Arterivirus (classification)</term>
<term>Arterivirus (genetics)</term>
<term>Arterivirus (metabolism)</term>
<term>Binding Sites</term>
<term>Cloning, Molecular</term>
<term>Coronavirus (chemistry)</term>
<term>Coronavirus (classification)</term>
<term>Coronavirus (genetics)</term>
<term>Coronavirus (metabolism)</term>
<term>Crystallography, X-Ray</term>
<term>Endoribonucleases (chemistry)</term>
<term>Endoribonucleases (genetics)</term>
<term>Endoribonucleases (metabolism)</term>
<term>Escherichia coli (genetics)</term>
<term>Escherichia coli (metabolism)</term>
<term>Evolution, Molecular</term>
<term>Gene Expression</term>
<term>Genetic Vectors (chemistry)</term>
<term>Genetic Vectors (metabolism)</term>
<term>Models, Molecular</term>
<term>Nidovirales (chemistry)</term>
<term>Nidovirales (classification)</term>
<term>Nidovirales (genetics)</term>
<term>Nidovirales (metabolism)</term>
<term>Protein Binding</term>
<term>Protein Conformation, alpha-Helical</term>
<term>Protein Conformation, beta-Strand</term>
<term>Protein Interaction Domains and Motifs</term>
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<term>Arterivirus (génétique)</term>
<term>Arterivirus (métabolisme)</term>
<term>Clonage moléculaire</term>
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<term>Coronavirus (génétique)</term>
<term>Coronavirus (métabolisme)</term>
<term>Cristallographie aux rayons X</term>
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<term>Endoribonucleases (génétique)</term>
<term>Endoribonucleases (métabolisme)</term>
<term>Escherichia coli (génétique)</term>
<term>Escherichia coli (métabolisme)</term>
<term>Expression des gènes</term>
<term>Liaison aux protéines</term>
<term>Modèles moléculaires</term>
<term>Motifs et domaines d'intéraction protéique</term>
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<term>Crystallography, X-Ray</term>
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<term>Sequence Alignment</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term>
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<term>Clonage moléculaire</term>
<term>Coronavirus</term>
<term>Cristallographie aux rayons X</term>
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<term>Modèles moléculaires</term>
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<front><div type="abstract" xml:lang="en">Nidovirus endoribonucleases (NendoUs) include nonstructural protein 15 (nsp15) from coronaviruses and nsp11 from arteriviruses, both of which have been reported to participate in the viral replication process and in the evasion of the host immune system. Results from a previous study of coronaviruses SARS-CoV, HCoV-229E, and MHV nsp15 indicate that it mainly forms a functional hexamer, whereas nsp11 from the arterivirus PRRSV is a dimer. Here, we found that porcine <i>Deltacoronavirus</i>
(PDCoV) nsp15 primarily exists as dimers and monomers <i>in vitro</i>
Biological experiments reveal that a PDCoV nsp15 mutant lacking the first 27 amino acids of the N-terminal domain (Asn-1-Asn-27) forms more monomers and displays decreased enzymatic activity, indicating that this region is important for its dimerization. Moreover, multiple sequence alignments and three-dimensional structural analysis indicated that the C-terminal region (His-251-Val-261) of PDCoV nsp15 is 10 amino acids shorter and forms a shorter loop than that formed by the equivalent sequence (Gln-259-Phe-279) of SARS-CoV nsp15. This result may explain why PDCoV nsp15 failed to form hexamers. We speculate that NendoUs may have originated from XendoU endoribonucleases (XendoUs) forming monomers in eukaryotic cells, that NendoU from arterivirus gained the ability to form dimers, and that the coronavirus variants then evolved the capacity to assemble into hexamers. We further propose that PDCoV nsp15 may be an intermediate in this evolutionary process. Our findings provide a theoretical basis for improving our understanding of NendoU evolution and offer useful clues for designing drugs and vaccines against nidoviruses.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29887523</PMID>
<DateCompleted><Year>2019</Year>
<Month>02</Month>
<Day>08</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>03</Month>
<Day>26</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>293</Volume>
<Issue>31</Issue>
<PubDate><Year>2018</Year>
<Month>08</Month>
<Day>03</Day>
</PubDate>
</JournalIssue>
<Title>The Journal of biological chemistry</Title>
<ISOAbbreviation>J. Biol. Chem.</ISOAbbreviation>
</Journal>
<ArticleTitle>Insight into the evolution of nidovirus endoribonuclease based on the finding that nsp15 from porcine <i>Deltacoronavirus</i>
functions as a dimer.</ArticleTitle>
<Pagination><MedlinePgn>12054-12067</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.RA118.003756</ELocationID>
<Abstract><AbstractText>Nidovirus endoribonucleases (NendoUs) include nonstructural protein 15 (nsp15) from coronaviruses and nsp11 from arteriviruses, both of which have been reported to participate in the viral replication process and in the evasion of the host immune system. Results from a previous study of coronaviruses SARS-CoV, HCoV-229E, and MHV nsp15 indicate that it mainly forms a functional hexamer, whereas nsp11 from the arterivirus PRRSV is a dimer. Here, we found that porcine <i>Deltacoronavirus</i>
(PDCoV) nsp15 primarily exists as dimers and monomers <i>in vitro</i>
Biological experiments reveal that a PDCoV nsp15 mutant lacking the first 27 amino acids of the N-terminal domain (Asn-1-Asn-27) forms more monomers and displays decreased enzymatic activity, indicating that this region is important for its dimerization. Moreover, multiple sequence alignments and three-dimensional structural analysis indicated that the C-terminal region (His-251-Val-261) of PDCoV nsp15 is 10 amino acids shorter and forms a shorter loop than that formed by the equivalent sequence (Gln-259-Phe-279) of SARS-CoV nsp15. This result may explain why PDCoV nsp15 failed to form hexamers. We speculate that NendoUs may have originated from XendoU endoribonucleases (XendoUs) forming monomers in eukaryotic cells, that NendoU from arterivirus gained the ability to form dimers, and that the coronavirus variants then evolved the capacity to assemble into hexamers. We further propose that PDCoV nsp15 may be an intermediate in this evolutionary process. Our findings provide a theoretical basis for improving our understanding of NendoU evolution and offer useful clues for designing drugs and vaccines against nidoviruses.</AbstractText>
<CopyrightInformation>© 2018 Zheng et al.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zheng</LastName>
<ForeName>Anjun</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>From the State Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Key Laboratory of Preventive Veterinary Medicine in Hubei Province, The Cooperative Innovation Center for Sustainable Pig Production, and.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Shi</LastName>
<ForeName>Yuejun</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>From the State Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Key Laboratory of Preventive Veterinary Medicine in Hubei Province, The Cooperative Innovation Center for Sustainable Pig Production, and.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, China and.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Shen</LastName>
<ForeName>Zhou</ForeName>
<Initials>Z</Initials>
<AffiliationInfo><Affiliation>From the State Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Key Laboratory of Preventive Veterinary Medicine in Hubei Province, The Cooperative Innovation Center for Sustainable Pig Production, and.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wang</LastName>
<ForeName>Gang</ForeName>
<Initials>G</Initials>
<AffiliationInfo><Affiliation>From the State Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Key Laboratory of Preventive Veterinary Medicine in Hubei Province, The Cooperative Innovation Center for Sustainable Pig Production, and.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Shi</LastName>
<ForeName>Jiale</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>From the State Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Key Laboratory of Preventive Veterinary Medicine in Hubei Province, The Cooperative Innovation Center for Sustainable Pig Production, and.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Xiong</LastName>
<ForeName>Qiqi</ForeName>
<Initials>Q</Initials>
<AffiliationInfo><Affiliation>College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, China and.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Fang</LastName>
<ForeName>Liurong</ForeName>
<Initials>L</Initials>
<AffiliationInfo><Affiliation>From the State Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Key Laboratory of Preventive Veterinary Medicine in Hubei Province, The Cooperative Innovation Center for Sustainable Pig Production, and.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Xiao</LastName>
<ForeName>Shaobo</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>From the State Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Key Laboratory of Preventive Veterinary Medicine in Hubei Province, The Cooperative Innovation Center for Sustainable Pig Production, and.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Fu</LastName>
<ForeName>Zhen F</ForeName>
<Initials>ZF</Initials>
<AffiliationInfo><Affiliation>the Department of Pathology, College of Veterinary Medicine, University of Georgia, Athens, Georgia 30602.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Peng</LastName>
<ForeName>Guiqing</ForeName>
<Initials>G</Initials>
<AffiliationInfo><Affiliation>From the State Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, penggq@mail.hzau.edu.cn.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Key Laboratory of Preventive Veterinary Medicine in Hubei Province, The Cooperative Innovation Center for Sustainable Pig Production, and.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
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<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2018</Year>
<Month>06</Month>
<Day>10</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>J Biol Chem</MedlineTA>
<NlmUniqueID>2985121R</NlmUniqueID>
<ISSNLinking>0021-9258</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D021122">Protein Subunits</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance>
</Chemical>
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<NameOfSubstance UI="D017361">Viral Nonstructural Proteins</NameOfSubstance>
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<Chemical><RegistryNumber>EC 3.1.-</RegistryNumber>
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<Chemical><RegistryNumber>EC 3.1.-</RegistryNumber>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018018" MajorTopicYN="N">Arterivirus</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000145" MajorTopicYN="N">classification</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017934" MajorTopicYN="N">Coronavirus</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000145" MajorTopicYN="N">classification</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</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="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D019143" MajorTopicYN="N">Evolution, Molecular</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015870" MajorTopicYN="N">Gene Expression</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005822" MajorTopicYN="N">Genetic Vectors</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D028381" MajorTopicYN="N">Nidovirales</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000145" MajorTopicYN="N">classification</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000072756" MajorTopicYN="N">Protein Conformation, alpha-Helical</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000072757" MajorTopicYN="N">Protein Conformation, beta-Strand</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D054730" MajorTopicYN="N">Protein Interaction Domains and Motifs</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D021122" MajorTopicYN="N">Protein Subunits</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="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="Q000145" MajorTopicYN="N">classification</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="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</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>
<MeshHeading><DescriptorName UI="D014779" MajorTopicYN="N">Virus Replication</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">PDCoV nsp15</Keyword>
<Keyword MajorTopicYN="Y">endoribonuclease</Keyword>
<Keyword MajorTopicYN="Y">evolution</Keyword>
<Keyword MajorTopicYN="Y">nidovirus</Keyword>
<Keyword MajorTopicYN="Y">oligomerization</Keyword>
<Keyword MajorTopicYN="Y">protein evolution</Keyword>
<Keyword MajorTopicYN="Y">protein purification</Keyword>
<Keyword MajorTopicYN="Y">viral protein</Keyword>
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<affiliations><list><country><li>République populaire de Chine</li>
<li>États-Unis</li>
</country>
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<tree><noCountry><name sortKey="Fang, Liurong" sort="Fang, Liurong" uniqKey="Fang L" first="Liurong" last="Fang">Liurong Fang</name>
<name sortKey="Shen, Zhou" sort="Shen, Zhou" uniqKey="Shen Z" first="Zhou" last="Shen">Zhou Shen</name>
<name sortKey="Shi, Jiale" sort="Shi, Jiale" uniqKey="Shi J" first="Jiale" last="Shi">Jiale Shi</name>
<name sortKey="Shi, Yuejun" sort="Shi, Yuejun" uniqKey="Shi Y" first="Yuejun" last="Shi">Yuejun Shi</name>
<name sortKey="Wang, Gang" sort="Wang, Gang" uniqKey="Wang G" first="Gang" last="Wang">Gang Wang</name>
<name sortKey="Xiao, Shaobo" sort="Xiao, Shaobo" uniqKey="Xiao S" first="Shaobo" last="Xiao">Shaobo Xiao</name>
<name sortKey="Xiong, Qiqi" sort="Xiong, Qiqi" uniqKey="Xiong Q" first="Qiqi" last="Xiong">Qiqi Xiong</name>
<name sortKey="Zheng, Anjun" sort="Zheng, Anjun" uniqKey="Zheng A" first="Anjun" last="Zheng">Anjun Zheng</name>
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<country name="États-Unis"><region name="Géorgie (États-Unis)"><name sortKey="Fu, Zhen F" sort="Fu, Zhen F" uniqKey="Fu Z" first="Zhen F" last="Fu">Zhen F. Fu</name>
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<country name="République populaire de Chine"><noRegion><name sortKey="Peng, Guiqing" sort="Peng, Guiqing" uniqKey="Peng G" first="Guiqing" last="Peng">Guiqing Peng</name>
</noRegion>
</country>
</tree>
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