Evidence map›Paper›PMID 30044982›Full record

ArticleCell reports2018

N-Terminal Acetylation by NatB Is Required for the Shutoff Activity of Influenza A Virus PA-X.

Kohei Oishi, Seiya Yamayoshi, Hiroko Kozuka-Hata, Masaaki Oyama, Yoshihiro Kawaoka

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.8field-weighted citation impact, top 7% 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

39 citing papers in PubMed, 59 citations in OpenAlex.

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  14. HAP1, a new revolutionary cell model for gene editing using CRISPR-Cas9.Frontiers in cell and developmental biology · 2023
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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

5 authors at 2 institutions in 2 countries.

Kohei OishiDivision of Virology, Department of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, Tokyo 108-8639, Japan.
Seiya YamayoshiDivision of Virology, Department of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, Tokyo 108-8639, Japan. Electronic address: yamayo@ims.u-tokyo.ac.jp.
Hiroko Kozuka-HataMedical Proteomics Laboratory, Institution of Medical Science, University of Tokyo, Tokyo 108-8639, Japan.
Masaaki OyamaMedical Proteomics Laboratory, Institution of Medical Science, University of Tokyo, Tokyo 108-8639, Japan.
Yoshihiro KawaokaDivision of Virology, Department of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, Tokyo 108-8639, Japan; Department of Pathobiological Sciences, School of Veterinary Medicine, University of Wisconsin-Madison, Madison, WI 53711, USA; Department of Special Pathogens, International Research Center for Infectious Diseases, Institute of Medical Science, University of Tokyo, Tokyo 108-8639, Japan. Electronic address: kawaokay@svm.vetmed.wisc.edu.
The University of Tokyo · JPUniversity of Wisconsin–Madison · US

Funding

Study of Novel HHV8/KSHV Encoded GenesU19AI107810 · NIAID · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DITTMER, DIRK P · 2013 to 2017
$10.6M
NIAID NIH HHS U19 AI107810
6 · The paper itself

Abstract

N-terminal acetylation is a major posttranslational modification in eukaryotes catalyzed by N-terminal acetyltransferases (NATs), NatA through NatF. Although N-terminal acetylation modulates diverse protein functions, little is known about its roles in virus replication. We found that NatB, which comprises NAA20 and NAA25, is involved in the shutoff activity of influenza virus PA-X. The shutoff activity of PA-X was suppressed in NatB-deficient cells, and PA-X mutants that are not acetylated by NatB showed reduced shutoff activities. We also evaluated the importance of N-terminal acetylation of PA, because PA-X shares its N-terminal sequence with PA. Viral polymerase activity was reduced in NatB-deficient cells. Moreover, mutant PAs that are not acetylated by NatB lost their function in the viral polymerase complex. Taken together, our findings demonstrate that N-terminal acetylation is required for the shutoff activity of PA-X and for viral polymerase activity.

Indexed as

AcetylationAcetyltransferasesHEK293 CellsHumansInfluenza A virusRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsViral Nonstructural ProteinsAcetyltransferasesNatB protein, S cerevisiaePA-X protein, influenza A virusRepressor ProteinsSaccharomyces cerevisiae ProteinsViral Nonstructural Proteins

Identifiers

PMID30044982
PMCPMC6296758
OpenAlexW2883357866

What OpenQuestion holds

Textmetadata
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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.