Evidence map›Paper›PMID 28003482›Full record

ArticleJournal of virology2017

NS1 Protein Amino Acid Changes D189N and V194I Affect Interferon Responses, Thermosensitivity, and Virulence of Circulating H3N2 Human Influenza A Viruses.

Aitor Nogales, Luis Martinez-Sobrido, David J Topham, Marta L DeDiego

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

38 citing papers in PubMed, 53 citations in OpenAlex.

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  16. Immunity to Influenza Infection in Humans.Cold Spring Harbor perspectives in medicine · 2021
    Review
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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

4 authors at 1 institution in 1 country.

Aitor NogalesDepartment of Microbiology and Immunology, University of Rochester, Rochester, New York, USA.
Luis Martinez-SobridoDepartment of Microbiology and Immunology, University of Rochester, Rochester, New York, USA.
David J TophamDavid H. Smith Center for Vaccine Biology and Immunology, University of Rochester, Rochester, New York, USA David_Topham@URMC.rochester.edu Marta_Lopez@URMC.rochester.edu.ORCID http://orcid.org/0000-0002-9435-8673
Marta L DeDiegoDavid H. Smith Center for Vaccine Biology and Immunology, University of Rochester, Rochester, New York, USA David_Topham@URMC.rochester.edu Marta_Lopez@URMC.rochester.edu.
University of Rochester · US

Funding

Tissue regulation of T cell function - Reagents CoreP01AI102851 · NIAID · UNIVERSITY OF ROCHESTER · PI Deborah J Fowell · 2014 to 2026
$26.0M
NIAID NIH HHS HHSN266200700008CNIAID NIH HHS P01 AI102851
6 · The paper itself

Abstract

Influenza virus NS1 protein is a nonstructural, multifunctional protein that counteracts host innate immune responses, modulating virus pathogenesis. NS1 protein variability in subjects infected with H3N2 influenza A viruses (IAVs) during the 2010/2011 season was analyzed, and amino acid changes in residues 86, 189, and 194 were found. The consequences of these mutations for the NS1-mediated inhibition of IFN responses and the pathogenesis of the virus were evaluated, showing that NS1 mutations D189N and V194I impaired the ability of the NS1 protein to inhibit general gene expression, most probably because these mutations decreased the binding of NS1 to the cleavage and polyadenylation specificity factor 30 (CPSF30). A recombinant A/Puerto Rico/8/34 (PR8) H1N1 virus encoding the H3N2 NS1-D189N protein was slightly attenuated, whereas the virus encoding the H3N2 NS1-V194I protein was further attenuated in mice. The higher attenuation of this virus could not be explained by differences in the ability of the two NS1 proteins to counteract host innate immune responses, indicating that another factor must be responsible. In fact, we showed that the virus encoding the H3N2 NS1-V194I protein demonstrated a temperature-sensitive (ts) phenotype, providing a most likely explanation for the stronger attenuation observed. As far as we know, this is the first description of a mutation in NS1 residue 194 conferring a ts phenotype. These studies are relevant in order to identify new residues important for NS1 functions and in human influenza virus surveillance to assess mutations affecting the pathogenicity of circulating viruses.

Indexed as

A549 CellsAmino Acid SequenceAmino Acid SubstitutionAnimalsChlorocebus aethiopsCleavage And Polyadenylation Specificity FactorDogsFemaleHEK293 CellsHumansImmunity, InnateInfluenza A Virus, H3N2 SubtypeInfluenza, HumanInterferonsMadin Darby Canine Kidney CellsMice, Inbred C57BLCleavage And Polyadenylation Specificity FactorCPSF4 protein, humanINS1 protein, influenza virusInterferonsViral Nonstructural Proteinsantiviral responseinfluenza virusinnate immunityNS1 proteinpathogenesisvirus-host interactions

Identifiers

PMID28003482
PMCPMC5309952
OpenAlexW2561408151

What OpenQuestion holds

Textmetadata
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.