{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["285(22)"],"submitter":["Wunderlich K"],"pubmed_abstract":["Despite their close phylogenetic relationship, natural intertypic reassortants between influenza A (FluA) and B (FluB) viruses have not been described. Inefficient polymerase assembly of the three polymerase subunits may contribute to this incompatibility, especially because the known protein-protein interaction domains, including the PA-binding domain of PB1, are highly conserved for each virus type. Here we show that substitution of the FluA PA-binding domain (PB1-A(1-25)) with that of FluB (PB1-B(1-25)) is accompanied by reduced polymerase activity and viral growth of FluA. Consistent with these findings, surface plasmon resonance spectroscopy measurements revealed that PA of FluA exhibits impaired affinity to biotinylated PB1-B(1-25) peptides. PA of FluB showed no detectable affinity t"],"journal":["The Journal of biological chemistry"],"pagination":["16704-12"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2878059"],"repository":["biostudies-literature"],"pubmed_title":["Limited compatibility of polymerase subunit interactions in influenza A and B viruses."],"pmcid":["PMC2878059"],"pubmed_authors":["Wolff T","Schwemmle M","Wunderlich K","Juozapaitis M","Mayer D","Zohner A","Manz B","Gotz V","Martin A"],"additional_accession":[]},"is_claimable":false,"name":"Limited compatibility of polymerase subunit interactions in influenza A and B viruses.","description":"Despite their close phylogenetic relationship, natural intertypic reassortants between influenza A (FluA) and B (FluB) viruses have not been described. Inefficient polymerase assembly of the three polymerase subunits may contribute to this incompatibility, especially because the known protein-protein interaction domains, including the PA-binding domain of PB1, are highly conserved for each virus type. Here we show that substitution of the FluA PA-binding domain (PB1-A(1-25)) with that of FluB (PB1-B(1-25)) is accompanied by reduced polymerase activity and viral growth of FluA. Consistent with these findings, surface plasmon resonance spectroscopy measurements revealed that PA of FluA exhibits impaired affinity to biotinylated PB1-B(1-25) peptides. PA of FluB showed no detectable affinity t","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 May","modification":"2026-05-05T02:43:48.442Z","creation":"2019-03-27T00:31:11Z"},"accession":"S-EPMC2878059","cross_references":{"pubmed":["20363752"],"doi":["10.1074/jbc.M110.102533","10.1074/jbc.m110.102533"]}}