Evidence map›Paper›PMID 30227889›Full record

ArticleBMC research notes2018

Effects of mutations in the effector domain of influenza A virus NS1 protein.

Carina F Pereira, Helen M Wise, Dominic Kurian, Rute M Pinto, Maria J Amorim, Andrew C Gill, Paul Digard

Open access · goldAbstract read
In one paragraph

Article in BMC research notes, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.8field-weighted citation impact, top 26% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed, 9 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 4 countries.

Carina F PereiraDivision of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, UK.
Helen M WiseDivision of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, UK.
Dominic KurianThe Roslin Institute, University of Edinburgh, Easter Bush, Midlothian, EH25 9RG, UK.
Rute M PintoThe Roslin Institute, University of Edinburgh, Easter Bush, Midlothian, EH25 9RG, UK.
Maria J AmorimDivision of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, UK.
Andrew C GillThe Roslin Institute, University of Edinburgh, Easter Bush, Midlothian, EH25 9RG, UK.
Paul DigardDivision of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, UK. paul.digard@roslin.ed.ac.uk.ORCID http://orcid.org/0000-0002-0872-9440
Roslin Institute · GBUniversity of Cambridge · GB

Funding

Biotechnology and Biological Sciences Research Council BBS/E/D/20002173Biotechnology and Biological Sciences Research Council BBS/E/D/20241864Fundação para a Ciência e a Tecnologia IF/00899/2013Fundação para a Ciência e a Tecnologia SFRH/BD/60299/2009
6 · The paper itself

Abstract

objectiveThe 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.

resultsThe 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.

Indexed as

MutationActive Transport, Cell NucleusInfluenza A virusProtein BindingProtein FoldingRNA, MessengerViral Nonstructural ProteinsINS1 protein, influenza virusRNA, MessengerViral Nonstructural ProteinsInfluenza A virusNS1Nuclear exportPI3KRIG-ITrim25

Identifiers

PMID30227889
PMCPMC6145200
OpenAlexW2885478293

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.