An interactome map of the nucleocapsid protein from a highly pathogenic North American porcine reproductive and respiratory syndrome virus strain generated using SILAC‐based quantitative proteomics
Identifieur interne : 001F34 ( Main/Exploration ); précédent : 001F33; suivant : 001F35An interactome map of the nucleocapsid protein from a highly pathogenic North American porcine reproductive and respiratory syndrome virus strain generated using SILAC‐based quantitative proteomics
Auteurs : Stefanie S. Jourdan [Royaume-Uni] ; Fernando Osorio [États-Unis] ; Julian A. Hiscox [Royaume-Uni]Source :
- PROTEOMICS [ 1615-9853 ] ; 2012-04.
English descriptors
- Teeft :
- Attenuating mutations, Background binding, Binding protein, Binding ratio, Bioinformatic analysis, Biological replicates, Biological sciences, Cell lysates, Cellular, Cellular biology, Cellular protein, Cellular proteins, Coronavirus, Coronavirus genome, Dataset, Egfp, Eukaryotic translation initiation factor, Gene expression, Gene name protein name egfp, Genome, Gmbh, Growth factor, Helicase, Hnrnp particles, Information table, Ingenuity pathway analysis, Interaction database, Interactome, Kgaa, More peptides, Mouse hepatitis virus, Mrna, Mrna stability, Nuclear ribonucleoprotein, Nucleic acids, Nucleocapsid, Nucleocapsid protein, Nucleolus, Peptide, Porcine, Posterior error probability, Pride converter, Protein, Protein function, Protein synthesis, Proteomics, Proteomics analysis, Prrsv, Quantitative proteomic analysis, Recombinant vaccines, Replication, Respiratory syndrome virus, Respiratory syndrome virus nucleocapsid protein, Respiratory syndrome virus strain, Ribonucleoprotein, Stable isotope, Syndrome, Translation initiation, Uorescent protein, Vaccine, Vaccine strains, Verlag, Verlag gmbh, Vero cells, Viral, Virol, Virology, Virus, Virus replication, Weinheim, Western blot.
Abstract
Positive strand RNA viruses replicate in the cytoplasm of an infected cell and encode nucleocapsid proteins. These proteins function to promote encapsidation of the RNA genome and virus particle assembly as well as playing potential roles in viral RNA synthesis. Nucleocapsid proteins can also associate with cellular proteins and signaling cascades. The arterivirus nucleocapsid (N) protein is no exception and localizes to both the cytoplasm and the nucleolus in virus‐infected cells. This study generated an interactome map of the N protein from a highly virulent North American strain of porcine reproductive and respiratory syndrome virus (PRRSV). This is a major pathogen of swine resulting in significant morbidity and mortality. Crucial to the study was the use of SILAC coupled to affinity purification using GFP‐traps and LC‐MS/MS. This approach has not been applied before to the investigation of host/viral protein interactomes and this study revealed that the PRRSV N protein interacts with the host cell protein synthesis machinery especially at the level of translation initiation as well as with the RNA post‐transcriptional modification machinery. Applications of the dataset can include studies of virus/host interactions and the design of live attenuated recombinant vaccines.
Url:
DOI: 10.1002/pmic.201100469
Affiliations:
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These proteins function to promote encapsidation of the RNA genome and virus particle assembly as well as playing potential roles in viral RNA synthesis. Nucleocapsid proteins can also associate with cellular proteins and signaling cascades. The arterivirus nucleocapsid (N) protein is no exception and localizes to both the cytoplasm and the nucleolus in virus‐infected cells. This study generated an interactome map of the N protein from a highly virulent North American strain of porcine reproductive and respiratory syndrome virus (PRRSV). This is a major pathogen of swine resulting in significant morbidity and mortality. Crucial to the study was the use of SILAC coupled to affinity purification using GFP‐traps and LC‐MS/MS. This approach has not been applied before to the investigation of host/viral protein interactomes and this study revealed that the PRRSV N protein interacts with the host cell protein synthesis machinery especially at the level of translation initiation as well as with the RNA post‐transcriptional modification machinery. Applications of the dataset can include studies of virus/host interactions and the design of live attenuated recombinant vaccines.</div></front></TEI><affiliations><list><country><li>Royaume-Uni</li><li>États-Unis</li></country><region><li>Angleterre</li><li>Yorkshire-et-Humber</li></region><settlement><li>Leeds</li></settlement><orgName><li>Université de Leeds</li></orgName></list><tree><country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Jourdan, Stefanie S" sort="Jourdan, Stefanie S" uniqKey="Jourdan S" first="Stefanie S." last="Jourdan">Stefanie S. Jourdan</name></region><name sortKey="Hiscox, Julian A" sort="Hiscox, Julian A" uniqKey="Hiscox J" first="Julian A." last="Hiscox">Julian A. Hiscox</name><name sortKey="Hiscox, Julian A" sort="Hiscox, Julian A" uniqKey="Hiscox J" first="Julian A." last="Hiscox">Julian A. Hiscox</name><name sortKey="Hiscox, Julian A" sort="Hiscox, Julian A" uniqKey="Hiscox J" first="Julian A." last="Hiscox">Julian A. Hiscox</name></country><country name="États-Unis"><noRegion><name sortKey="Osorio, Fernando" sort="Osorio, Fernando" uniqKey="Osorio F" first="Fernando" last="Osorio">Fernando Osorio</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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