<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>285(22)</volume><submitter>Wunderlich K</submitter><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</pubmed_abstract><journal>The Journal of biological chemistry</journal><pagination>16704-12</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2878059</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Limited compatibility of polymerase subunit interactions in influenza A and B viruses.</pubmed_title><pmcid>PMC2878059</pmcid><pubmed_authors>Wolff T</pubmed_authors><pubmed_authors>Schwemmle M</pubmed_authors><pubmed_authors>Wunderlich K</pubmed_authors><pubmed_authors>Juozapaitis M</pubmed_authors><pubmed_authors>Mayer D</pubmed_authors><pubmed_authors>Zohner A</pubmed_authors><pubmed_authors>Manz B</pubmed_authors><pubmed_authors>Gotz V</pubmed_authors><pubmed_authors>Martin A</pubmed_authors></additional><is_claimable>false</is_claimable><name>Limited compatibility of polymerase subunit interactions in influenza A and B viruses.</name><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</description><dates><release>2010-01-01T00:00:00Z</release><publication>2010 May</publication><modification>2026-05-05T02:43:48.442Z</modification><creation>2019-03-27T00:31:11Z</creation></dates><accession>S-EPMC2878059</accession><cross_references><pubmed>20363752</pubmed><doi>10.1074/jbc.M110.102533</doi><doi>10.1074/jbc.m110.102533</doi></cross_references></HashMap>