Evidence map›Paper›PMID 24603811›Full record

ArticlePLoS pathogens2014

The hypervariable amino-terminus of P1 protease modulates potyviral replication and host defense responses.

Fabio Pasin, Carmen Simón-Mateo, Juan Antonio García

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
10.7field-weighted citation impact, top 2% 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

55 citing papers in PubMed, 115 citations in OpenAlex.

  1. Article
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  10. Article
  11. Role of Plant Virus Movement Proteins in Suppression of Host RNAi Defense.International journal of molecular sciences · 2023
    Review
  12. The Mechanism of Resistance of EUROPEAN Plum toPlants (Basel, Switzerland) · 2023
    Article
  13. Mapping allosteric pathway in NIa-Pro using computational approach.Quantitative biology (Beijing, China) · 2023
    Article
  14. Article
  15. Article
  16. AlkB RNA demethylase homologues and NMolecular plant pathology · 2022
    Article
  17. Article
  18. Review
  19. Article
  20. Water Deficit Improves Reproductive Fitness inPlants (Basel, Switzerland) · 2022
    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

3 authors at 1 institution in 1 country.

Fabio PasinDepartamento de Genética Molecular de Plantas, Centro Nacional de Biotecnología (CNB-CSIC), Madrid, Spain.
Carmen Simón-MateoDepartamento de Genética Molecular de Plantas, Centro Nacional de Biotecnología (CNB-CSIC), Madrid, Spain.
Juan Antonio GarcíaDepartamento de Genética Molecular de Plantas, Centro Nacional de Biotecnología (CNB-CSIC), Madrid, Spain.
Centro Nacional de Biotecnología · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The replication of many RNA viruses involves the translation of polyproteins, whose processing by endopeptidases is a critical step for the release of functional subunits. P1 is the first protease encoded in plant potyvirus genomes; once activated by an as-yet-unknown host factor, it acts in cis on its own C-terminal end, hydrolyzing the P1-HCPro junction. Earlier research suggests that P1 cooperates with HCPro to inhibit host RNA silencing defenses. Using Plum pox virus as a model, we show that although P1 does not have a major direct role in RNA silencing suppression, it can indeed modulate HCPro function by its self-cleavage activity. To study P1 protease regulation, we used bioinformatic analysis and in vitro activity experiments to map the core C-terminal catalytic domain. We present evidence that the hypervariable region that precedes the protease domain is predicted as intrinsically disordered, and that it behaves as a negative regulator of P1 proteolytic activity in in vitro cleavage assays. In viral infections, removal of the P1 protease antagonistic regulator is associated with greater symptom severity, induction of salicylate-dependent pathogenesis-related proteins, and reduced viral loads. We suggest that fine modulation of a viral protease activity has evolved to keep viral amplification below host-detrimental levels, and thus to maintain higher long-term replicative capacity.

Indexed as

Amino Acid SequenceBlotting, WesternChromatography, LiquidHost-Parasite InteractionsMolecular Sequence DataNicotianaPeptide HydrolasesPlant DiseasesPotyvirusProtein Structure, TertiaryReverse Transcriptase Polymerase Chain ReactionSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationTandem Mass SpectrometryViral ProteinsVirus ReplicationPeptide HydrolasesViral Proteins

Identifiers

PMID24603811
PMCPMC3946448
OpenAlexW2047995004

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.