Evidence map›Paper›PMID 21625420›Full record

ArticlePloS one2011

PDlim2 selectively interacts with the PDZ binding motif of highly pathogenic avian H5N1 influenza A virus NS1.

Jia Yu, Xin Li, Yu Wang, Bo Li, Hongyue Li, Yapeng Li, Weihong Zhou, Cuizhu Zhang, Yingying Wang, Zihe Rao and 2 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

20 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. The unexpected versatility of ALP/Enigma family proteins.Frontiers in cell and developmental biology · 2022
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  9. Influenza A Virus-Host Protein Interactions Control Viral Pathogenesis.International journal of molecular sciences · 2017
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  11. Article
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  13. Review
  14. Ubiquitination-mediated regulation of interferon responses.Growth factors (Chur, Switzerland) · 2012
    Review
  15. Review
  16. Article
  17. Review
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  20. 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

12 authors at 2 institutions in 1 country.

Jia YuTianjin Key Laboratory of Protein Science, College of Life Sciences, Nankai University, Tianjin, China.
Xin Li
Yu Wang
Bo Li
Hongyue Li
Yapeng Li
Weihong Zhou
Cuizhu Zhang
Yingying Wang
Zihe Rao
Mark Bartlam
Youjia Cao
Nankai University · CNState Key Laboratory of Pollution Control and Resource Reuse · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The multi-functional NS1 protein of influenza A virus is a viral virulence determining factor. The last four residues at the C-terminus of NS1 constitute a type I PDZ domain binding motif (PBM). Avian influenza viruses currently in circulation carry an NS1 PBM with consensus sequence ESEV, whereas human influenza viruses bear an NS1 PBM with consensus sequence RSKV or RSEV. The PBM sequence of the influenza A virus NS1 is reported to contribute to high viral pathogenicity in animal studies. Here, we report the identification of PDlim2 as a novel binding target of the highly pathogenic avian influenza virus H5N1 strain with an NS1 PBM of ESEV (A/Chicken/Henan/12/2004/H5N1, HN12-NS1) by yeast two-hybrid screening. The interaction was confirmed by in vitro GST pull-down assays, as well as by in vivo mammalian two-hybrid assays and bimolecular fluorescence complementation assays. The binding was also confirmed to be mediated by the interaction of the PDlim2 PDZ domain with the NS1 PBM motif. Interestingly, our assays showed that PDlim2 bound specifically with HN12-NS1, but exhibited no binding to NS1 from a human influenza H1N1 virus bearing an RSEV PBM (A/Puerto Rico/8/34/H1N1, PR8-NS1). A crystal structure of the PDlim2 PDZ domain fused with the C-terminal hexapeptide from HN12-NS1, together with GST pull-down assays on PDlim2 mutants, reveals that residues Arg16 and Lys31 of PDlim2 are critical for the binding between PDlim2 and HN12-NS1. The identification of a selective binding target of HN12-NS1 (ESEV), but not PR8-NS1 (RSEV), enables us to propose a structural mechanism for the interaction between NS1 PBM and PDlim2 or other PDZ-containing proteins.

Indexed as

Amino Acid SequenceHeLa CellsHumansInfluenza A Virus, H1N1 SubtypeInfluenza A Virus, H5N1 SubtypeInfluenza, HumanLIM Domain ProteinsMicrofilament ProteinsMolecular Sequence DataPDZ DomainsPeptide FragmentsProtein ConformationTwo-Hybrid System TechniquesViral Nonstructural ProteinsINS1 protein, influenza virusLIM Domain ProteinsMicrofilament ProteinsPDLIM2 protein, humanPeptide FragmentsViral Nonstructural Proteins

Identifiers

PMID21625420
PMCPMC3100292
OpenAlexW1999583314

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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.