{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Bradel-Tretheway BG"],"funding":["NCRR NIH HHS","NIAID NIH HHS"],"pagination":["8569-81"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3165779"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["85(17)"],"pubmed_abstract":["The trimeric RNA polymerase complex (3P, for PA-PB1-PB2) of influenza A virus (IAV) is an important viral determinant of pathogenicity and host range restriction. Specific interactions of the polymerase complex with host proteins may be determining factors in both of these characteristics and play important roles in the viral life cycle. To investigate this question, we performed a comprehensive proteomic analysis of human host proteins associated with the polymerase of the well-characterized H5N1 Vietnam/1203/04 isolate. We identified over 400 proteins by liquid chromatography-tandem mass spectrometry (LC-MS/MS), of which over 300 were found to bind to the PA subunit alone. The most intriguing and novel finding was the large number of mitochondrial proteins (∼20%) that associated with the"],"journal":["Journal of virology"],"pubmed_title":["Comprehensive proteomic analysis of influenza virus polymerase complex reveals a novel association with mitochondrial proteins and RNA polymerase accessory factors."],"pmcid":["PMC3165779"],"funding_grant_id":["P51RR000166","HHSN266200700008C","HHSN272200800060C","P51 RR000166","U54 AI081680"],"pubmed_authors":["Stevenson C","Bradel-Tretheway BG","Mattiacio JL","Purdy D","Krasnoselsky A","Dewhurst S","Katze MG"],"additional_accession":[]},"is_claimable":false,"name":"Comprehensive proteomic analysis of influenza virus polymerase complex reveals a novel association with mitochondrial proteins and RNA polymerase accessory factors.","description":"The trimeric RNA polymerase complex (3P, for PA-PB1-PB2) of influenza A virus (IAV) is an important viral determinant of pathogenicity and host range restriction. Specific interactions of the polymerase complex with host proteins may be determining factors in both of these characteristics and play important roles in the viral life cycle. To investigate this question, we performed a comprehensive proteomic analysis of human host proteins associated with the polymerase of the well-characterized H5N1 Vietnam/1203/04 isolate. We identified over 400 proteins by liquid chromatography-tandem mass spectrometry (LC-MS/MS), of which over 300 were found to bind to the PA subunit alone. The most intriguing and novel finding was the large number of mitochondrial proteins (∼20%) that associated with the","dates":{"release":"2011-01-01T00:00:00Z","publication":"2011 Sep","modification":"2026-05-03T12:54:42.347Z","creation":"2025-07-01T03:05:44.278Z"},"accession":"S-EPMC3165779","cross_references":{"pubmed":["21715506"],"doi":["10.1128/JVI.00496-11","10.1128/jvi.00496-11"]}}