SARS coronavirus protein 7a interacts with human Ap4A-hydrolase.
Identifieur interne : 001602 ( PubMed/Checkpoint ); précédent : 001601; suivant : 001603SARS coronavirus protein 7a interacts with human Ap4A-hydrolase.
Auteurs : Natalia Vasilenko [Canada] ; Igor Moshynskyy ; Alexander ZakhartchoukSource :
- Virology journal [ 1743-422X ] ; 2010.
Descripteurs français
- KwdFr :
- Acid anhydride hydrolases (métabolisme), Cartographie d'interactions entre protéines, Cytoplasme (), Humains, Immunoprécipitation, Interactions hôte-pathogène, Liaison aux protéines, Lignée cellulaire, Microscopie confocale, Protéines de la matrice virale (métabolisme), Techniques de double hybride, Virus du SRAS (physiologie).
- MESH :
- métabolisme : Acid anhydride hydrolases, Protéines de la matrice virale.
- physiologie : Virus du SRAS.
- Cartographie d'interactions entre protéines, Cytoplasme, Humains, Immunoprécipitation, Interactions hôte-pathogène, Liaison aux protéines, Lignée cellulaire, Microscopie confocale, Techniques de double hybride.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Acid Anhydride Hydrolases, Viral Matrix Proteins.
- chemistry : Cytoplasm.
- physiology : SARS Virus.
- Cell Line, Host-Pathogen Interactions, Humans, Immunoprecipitation, Microscopy, Confocal, Protein Binding, Protein Interaction Mapping, Two-Hybrid System Techniques.
Abstract
The SARS coronavirus (SARS-CoV) open reading frame 7a (ORF 7a) encodes a 122 amino acid accessory protein. It has no significant sequence homology with any other known proteins. The 7a protein is present in the virus particle and has been shown to interact with several host proteins; thereby implicating it as being involved in several pathogenic processes including apoptosis, inhibition of cellular protein synthesis, and activation of p38 mitogen activated protein kinase. In this study we present data demonstrating that the SARS-CoV 7a protein interacts with human Ap4A-hydrolase (asymmetrical diadenosine tetraphosphate hydrolase, EC 3.6.1.17). Ap4A-hydrolase is responsible for metabolizing the "allarmone" nucleotide Ap4A and therefore likely involved in regulation of cell proliferation, DNA replication, RNA processing, apoptosis and DNA repair. The interaction between 7a and Ap4A-hydrolase was identified using yeast two-hybrid screening. The interaction was confirmed by co-immunoprecipitation from cultured human cells transiently expressing V5-His tagged 7a and HA tagged Ap4A-hydrolase. Human tissue culture cells transiently expressing 7a and Ap4A-hydrolase tagged with EGFP and Ds-Red2 respectively show these proteins co-localize in the cytoplasm.
DOI: 10.1186/1743-422X-7-31
PubMed: 20144233
Affiliations:
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last="Vasilenko">Natalia Vasilenko</name><affiliation wicri:level="1"><nlm:affiliation>Vaccine and Infectious Disease Organization (VIDO), University of Saskatchewan, 120 Veterinary Road, Saskatoon, SK S7N5E3, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Vaccine and Infectious Disease Organization (VIDO), University of Saskatchewan, 120 Veterinary Road, Saskatoon, SK S7N5E3</wicri:regionArea><wicri:noRegion>SK S7N5E3</wicri:noRegion></affiliation></author><author><name sortKey="Moshynskyy, Igor" sort="Moshynskyy, Igor" uniqKey="Moshynskyy I" first="Igor" last="Moshynskyy">Igor Moshynskyy</name></author><author><name sortKey="Zakhartchouk, Alexander" sort="Zakhartchouk, Alexander" uniqKey="Zakhartchouk A" first="Alexander" last="Zakhartchouk">Alexander Zakhartchouk</name></author></analytic><series><title level="j">Virology journal</title><idno type="eISSN">1743-422X</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acid Anhydride Hydrolases (metabolism)</term><term>Cell Line</term><term>Cytoplasm (chemistry)</term><term>Host-Pathogen Interactions</term><term>Humans</term><term>Immunoprecipitation</term><term>Microscopy, Confocal</term><term>Protein Binding</term><term>Protein Interaction Mapping</term><term>SARS Virus (physiology)</term><term>Two-Hybrid System Techniques</term><term>Viral Matrix Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acid anhydride hydrolases (métabolisme)</term><term>Cartographie d'interactions entre protéines</term><term>Cytoplasme ()</term><term>Humains</term><term>Immunoprécipitation</term><term>Interactions hôte-pathogène</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Microscopie confocale</term><term>Protéines de la matrice virale (métabolisme)</term><term>Techniques de double hybride</term><term>Virus du SRAS (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Acid Anhydride Hydrolases</term><term>Viral Matrix Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Cytoplasm</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acid anhydride hydrolases</term><term>Protéines de la matrice virale</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line</term><term>Host-Pathogen Interactions</term><term>Humans</term><term>Immunoprecipitation</term><term>Microscopy, Confocal</term><term>Protein Binding</term><term>Protein Interaction Mapping</term><term>Two-Hybrid System Techniques</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cartographie d'interactions entre protéines</term><term>Cytoplasme</term><term>Humains</term><term>Immunoprécipitation</term><term>Interactions hôte-pathogène</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Microscopie confocale</term><term>Techniques de double hybride</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The SARS coronavirus (SARS-CoV) open reading frame 7a (ORF 7a) encodes a 122 amino acid accessory protein. It has no significant sequence homology with any other known proteins. The 7a protein is present in the virus particle and has been shown to interact with several host proteins; thereby implicating it as being involved in several pathogenic processes including apoptosis, inhibition of cellular protein synthesis, and activation of p38 mitogen activated protein kinase. In this study we present data demonstrating that the SARS-CoV 7a protein interacts with human Ap4A-hydrolase (asymmetrical diadenosine tetraphosphate hydrolase, EC 3.6.1.17). Ap4A-hydrolase is responsible for metabolizing the "allarmone" nucleotide Ap4A and therefore likely involved in regulation of cell proliferation, DNA replication, RNA processing, apoptosis and DNA repair. The interaction between 7a and Ap4A-hydrolase was identified using yeast two-hybrid screening. The interaction was confirmed by co-immunoprecipitation from cultured human cells transiently expressing V5-His tagged 7a and HA tagged Ap4A-hydrolase. Human tissue culture cells transiently expressing 7a and Ap4A-hydrolase tagged with EGFP and Ds-Red2 respectively show these proteins co-localize in the cytoplasm.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20144233</PMID><DateCompleted><Year>2010</Year><Month>04</Month><Day>21</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1743-422X</ISSN><JournalIssue CitedMedium="Internet"><Volume>7</Volume><PubDate><Year>2010</Year><Month>Feb</Month><Day>09</Day></PubDate></JournalIssue><Title>Virology journal</Title><ISOAbbreviation>Virol. J.</ISOAbbreviation></Journal><ArticleTitle>SARS coronavirus protein 7a interacts with human Ap4A-hydrolase.</ArticleTitle><Pagination><MedlinePgn>31</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1186/1743-422X-7-31</ELocationID><Abstract><AbstractText>The SARS coronavirus (SARS-CoV) open reading frame 7a (ORF 7a) encodes a 122 amino acid accessory protein. It has no significant sequence homology with any other known proteins. The 7a protein is present in the virus particle and has been shown to interact with several host proteins; thereby implicating it as being involved in several pathogenic processes including apoptosis, inhibition of cellular protein synthesis, and activation of p38 mitogen activated protein kinase. In this study we present data demonstrating that the SARS-CoV 7a protein interacts with human Ap4A-hydrolase (asymmetrical diadenosine tetraphosphate hydrolase, EC 3.6.1.17). Ap4A-hydrolase is responsible for metabolizing the "allarmone" nucleotide Ap4A and therefore likely involved in regulation of cell proliferation, DNA replication, RNA processing, apoptosis and DNA repair. The interaction between 7a and Ap4A-hydrolase was identified using yeast two-hybrid screening. The interaction was confirmed by co-immunoprecipitation from cultured human cells transiently expressing V5-His tagged 7a and HA tagged Ap4A-hydrolase. Human tissue culture cells transiently expressing 7a and Ap4A-hydrolase tagged with EGFP and Ds-Red2 respectively show these proteins co-localize in the cytoplasm.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Vasilenko</LastName><ForeName>Natalia</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Vaccine and Infectious Disease Organization (VIDO), University of Saskatchewan, 120 Veterinary Road, Saskatoon, SK S7N5E3, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Moshynskyy</LastName><ForeName>Igor</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Zakhartchouk</LastName><ForeName>Alexander</ForeName><Initials>A</Initials></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 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