Evidence map›Paper›PMID 26638129›Full record

ArticleMolecular plant pathology2016

The pathogenicity factor HrpF interacts with HrpA and HrpG to modulate type III secretion system (T3SS) function and t3ss expression in Pseudomonas syringae pv. averrhoi.

Yi-Chiao Huang, Yuan-Chuen Lin, Chia-Fong Wei, Wen-Ling Deng, Hsiou-Chen Huang

Open access · greenAbstract read
In one paragraph

Article in Molecular plant pathology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.0field-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

11 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Virulence-related regulatory network ofComputational and structural biotechnology journal · 2022
    Review
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  7. Regulation of theMicroorganisms · 2021
    Review
  8. Handling Poor Accrual in Pediatric Trials: A Simulation Study Using a Bayesian Approach.International journal of environmental research and public health · 2021
    Article
  9. Signal transduction schemes inComputational and structural biotechnology journal · 2020
    Review
  10. Article
  11. 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

5 authors at 1 institution in 1 country.

Yi-Chiao HuangDepartment of Plant Pathology, National Chung Hsing University, Taichung, 40227, Taiwan.
Yuan-Chuen LinGraduate Institute of Biotechnology, National Chung Hsing University, Taichung, 40227, Taiwan.
Chia-Fong WeiGraduate Institute of Biotechnology, National Chung Hsing University, Taichung, 40227, Taiwan.
Wen-Ling DengDepartment of Plant Pathology, National Chung Hsing University, Taichung, 40227, Taiwan.
Hsiou-Chen HuangGraduate Institute of Biotechnology, National Chung Hsing University, Taichung, 40227, Taiwan.
National Chung Hsing University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To ensure the optimal infectivity on contact with host cells, pathogenic Pseudomonas syringae has evolved a complex mechanism to control the expression and construction of the functional type III secretion system (T3SS) that serves as a dominant pathogenicity factor. In this study, we showed that the hrpF gene of P. syringae pv. averrhoi, which is located upstream of hrpG, encodes a T3SS-dependent secreted/translocated protein. Mutation of hrpF leads to the loss of bacterial ability on elicitation of disease symptoms in the host and a hypersensitive response in non-host plants, and the secretion or translocation of the tested T3SS substrates into the bacterial milieu or plant cells. Moreover, overexpression of hrpF in the wild-type results in delayed HR and reduced t3ss expression. The results of protein-protein interactions demonstrate that HrpF interacts directly with HrpG and HrpA in vitro and in vivo, and protein stability assays reveal that HrpF assists HrpA stability in the bacterial cytoplasm, which is reduced by a single amino acid substitution at the 67th lysine residue of HrpF with alanine. Taken together, the data presented here suggest that HrpF has two roles in the assembly of a functional T3SS: one by acting as a negative regulator, possibly involved in the HrpSVG regulation circuit via binding to HrpG, and the other by stabilizing HrpA in the bacterial cytoplasm via HrpF-HrpA interaction prior to the secretion and formation of Hrp pilus on the bacterial surface.

Indexed as

Type III Secretion SystemsAmino Acid SubstitutionBacterial ProteinsCytoplasmGene Expression Regulation, BacterialHost-Pathogen InteractionsImmunoprecipitationMutant ProteinsMutationNicotianaPhenotypePlant DiseasesProtein BindingProtein TransportPseudomonas syringaeRecombinant Fusion ProteinsBacterial ProteinsMutant ProteinsRecombinant Fusion ProteinsType III Secretion SystemshrpFPseudomonas syringaeT3SSt3ss regulation

Identifiers

PMID26638129
PMCPMC6638529
OpenAlexW2336542624

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.