The R35 residue of the influenza A virus NS1 protein has minimal effects on nuclear localization but alters virus replication through disrupting protein dimerization.

Erin N Lalime, Andrew Pekosz

Open access · greenAbstract read

In one paragraph

Article in Virology, 2014. 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

1.3field-weighted citation impact, top 21% 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, 12 citations in OpenAlex.

The ER-Golgi transport of influenza virus through NS1-Sec13 association during virus replication.Microbiology spectrum · 2024
Article
Cellular PSMB4 Protein Suppresses Influenza A Virus Replication through Targeting NS1 Protein.Viruses · 2022
Article
A Review and Meta-Analysis of Influenza Interactome Studies.Frontiers in microbiology · 2022
Review
Molecular Dynamics Simulations of Influenza A Virus NS1 Reveal a Remarkably Stable RNA-Binding Domain Harboring Promising Druggable Pockets.Viruses · 2020
Article
Mutations in the Influenza A Virus M1 Protein Enhance Virus Budding To Complement Lethal Mutations in the M2 Cytoplasmic Tail.Journal of virology · 2018
Article
Evaluation of the innate immune responses to influenza and live-attenuated influenza vaccine infection in primary differentiated human nasal epithelial cells.Vaccine · 2017
Article
Influenza A Virus Virulence Depends on Two Amino Acids in the N-Terminal Domain of Its NS1 Protein To Facilitate Inhibition of the RNA-Dependent Protein Kinase PKR.Journal of virology · 2017
Article

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

2 authors at 1 institution in 1 country.

Erin N LalimeW. Harry Feinstone Department of Molecular Microbiology and Immunology, Johns Hopkins University, Bloomberg School of Public Health, 615 North Wolfe Street, Suite E5132, Baltimore, MD 21205-2103, USA.

Andrew PekoszW. Harry Feinstone Department of Molecular Microbiology and Immunology, Johns Hopkins University, Bloomberg School of Public Health, 615 North Wolfe Street, Suite E5132, Baltimore, MD 21205-2103, USA. Electronic address: apekosz@jhsph.edu.

Johns Hopkins University · US

Funding

Training: Molecular & Cellular Bases of Infectious DiseasesT32AI007417 · NIAID · JOHNS HOPKINS UNIVERSITY · PI Arturo Casadevall · 1994 to 2026

$11.9M

NIAID NIH HHS T32 AI007417NIAID NIH HHS T32AI007417-19

6 · The paper itself

Abstract

The influenza A virus NS1 protein has a nuclear localization sequence (NLS) in the amino terminal region. This NLS overlaps sequences that are important for RNA binding as well as protein dimerization. To assess the significance of the NS1 NLS on influenza virus replication, the NLS amino acids were individually mutated to alanines and recombinant viruses encoding these mutations were rescued. Viruses containing NS1 proteins with mutations at R37, R38 and K41 displayed minimal changes in replication or NS1 protein nuclear localization. Recombinant viruses encoding NS1 R35A were not recovered but viruses containing second site mutations at position D39 in addition to the R35A mutation were isolated. The mutations at position 39 were shown to partially restore NS1 protein dimerization but had minimal effects on nuclear localization. These data indicate that the amino acids in the NS1 NLS region play a more important role in protein dimerization compared to nuclear localization.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAnimalsCell LineDogsGene Expression Regulation, ViralHumansInfluenza A virusMutagenesis, Site-DirectedMutationNuclear Localization SignalsProtein MultimerizationProtein TransportViral Nonstructural ProteinsVirus ReplicationINS1 protein, influenza virusNuclear Localization SignalsViral Nonstructural ProteinsDimerInfluenzaNS1Nuclear localizationRNA binding

Identifiers

PMID24928037

DOI10.1016/j.virol.2014.04.012

PMCPMC4095983

OpenAlexW1985947504

What OpenQuestion holds

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Registered trials

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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.