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dc.contributor.authorPatzina, Corinna
dc.contributor.authorBotting, Catherine H.
dc.contributor.authorGarcía-Sastre, Adolfo
dc.contributor.authorRandall, Richard E.
dc.contributor.authorHale, Benjamin G.
dc.identifier.citationPatzina , C , Botting , C H , García-Sastre , A , Randall , R E & Hale , B G 2017 , ' Human interactome of the influenza B virus NS1 protein ' , Journal of General Virology , vol. 98 , no. 9 , 000909 , pp. 2267-2273 .
dc.identifier.otherPURE: 251200799
dc.identifier.otherPURE UUID: e89173af-a0d8-4817-a82d-213daf9fdca0
dc.identifier.otherScopus: 85029595752
dc.identifier.otherPubMed: 28869005
dc.identifier.otherORCID: /0000-0002-9304-6678/work/60427043
dc.identifier.otherWOS: 000411713000006
dc.descriptionThis work was partially supported by NIAID grant U19AI106754, and by CRIP (Center for Research in Influenza Pathogenesis), an NIAID funded Center of Excellence for Influenza Research and Surveillance (CEIRS, contract #HHSN272201400008C) to A. G-S. Work at the University of Zurich was supported by the Swiss National Science Foundation (grant 31003A_159993 to BGH).en
dc.description.abstractNS1 proteins of influenza A and B viruses share limited sequence homology, yet both are potent manipulators of host cell processes, particularly interferon (IFN) induction. Although many cellular partners are reported for A/NS1, only a few (e.g. PKR and ISG15) have been identified for B/NS1. Here, affinity-purification and mass spectrometry were used to expand the known host interactome of B/NS1. We identified 22 human proteins as new putative targets for B/NS1, validating several, including DHX9, ILF3, YBX1 and HNRNPC. Consistent with two RNA-binding domains in B/NS1, many of the identified factors bind RNA and some interact with B/NS1 in an RNA-dependent manner. Functional characterization of several B/NS1 interactors identified SNRNP200 as a potential positive regulator of host IFN responses, while ILF3 exhibited dual roles in both IFN induction and influenza B virus replication. These data provide a resource for future investigations into the mechanisms underpinning host cell modulation by influenza B virus NS1.
dc.relation.ispartofJournal of General Virologyen
dc.rights© 2017 The Authors. This is an open access article under the terms of the, which permits unrestricted use, distribution and reproduction in any medium, provided the original author and source are credited.en
dc.subjectVirulence factoren
dc.subjectVirus-host interactionen
dc.subjectQR355 Virologyen
dc.titleHuman interactome of the influenza B virus NS1 proteinen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews.Biomedical Sciences Research Complexen
dc.contributor.institutionUniversity of St Andrews.School of Chemistryen
dc.contributor.institutionUniversity of St Andrews.EaSTCHEMen
dc.contributor.institutionUniversity of St Andrews.School of Biologyen
dc.description.statusPeer revieweden

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