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dc.contributor.authorPereira, Carina F
dc.contributor.authorWise, Helen M
dc.contributor.authorKurian, Dominic
dc.contributor.authorPinto, Rute M
dc.contributor.authorAmorim, Maria J
dc.contributor.authorGill, Andrew C
dc.contributor.authorDigard, Paul
dc.date.accessioned2018-09-19T06:02:35Z
dc.date.available2018-09-19T06:02:35Z
dc.date.issued2018-09-18
dc.identifier.citationBMC Research Notes. 2018 Sep 18;11(1):673
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/280333
dc.description.abstractAbstract Objective The multifunctional NS1 protein of influenza A virus has roles in antagonising cellular innate immune responses and promoting viral gene expression. To better understand the interplay between these functions, we tested the effects of NS1 effector domain mutations known to affect homo-dimerisation or interactions with cellular PI3 kinase or Trim25 on NS1 ability to promote nuclear export of viral mRNAs. Results The NS1 dimerisation mutant W187R retained the functions of binding cellular NXF1 as well as stabilising NXF1 interaction with viral segment 7 mRNAs and promoting their nuclear export. Two PI3K-binding mutants, NS1 Y89F and Y89A still bound NXF1 but no longer promoted NXF1 interactions with segment 7 mRNA or its nuclear export. The Trim25-binding mutant NS1 E96A/E97A bound NXF1 and supported NXF1 interactions with segment 7 mRNA but no longer supported mRNA nuclear export. Analysis of WT and mutant NS1 interaction partners identified hsp70 as specifically binding to NS1 E96A/E97A. Whilst these data suggest the possibility of functional links between NS1’s effects on intracellular signalling and its role in viral mRNA nuclear export, they also indicate potential pleiotropic effects of the NS1 mutations; in the case of E96A/E97A possibly via disrupted protein folding leading to chaperone recruitment.
dc.titleEffects of mutations in the effector domain of influenza A virus NS1 protein
dc.typeJournal Article
dc.date.updated2018-09-19T06:02:33Z
dc.language.rfc3066en
dc.rights.holderThe Author(s)
dc.identifier.doi10.17863/CAM.27706
rioxxterms.versionofrecord10.1186/s13104-018-3779-6


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