Evidence map›Paper›PMID 40195800›Full record

ArticleMolecular microbiology2025

PorA of the Type IX Secretion Is a Ligand of the PorXY Two-Component Regulatory System in Porphyromonas gingivalis.

Momoko Ito, Hideharu Yukitake, Paul D Veith, Dhana G Gorasia, Takashi Tominaga, Yuko Sasaki, Eric C Reynolds, Koji Nakayama, Mariko Naito, Mikio Shoji

Abstract read
In one paragraph

Article in Molecular microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Advances in the type IX secretion system: an exploration focusing onCurrent research in microbial sciences · 2025
    Review
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

10 authors.

Momoko ItoDepartment of Microbiology and Oral Infection, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki, Nagasaki, Japan.
Hideharu YukitakeDepartment of Microbiology and Oral Infection, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki, Nagasaki, Japan.
Paul D VeithOral Health Cooperative Research Centre, Melbourne Dental School, Bio21 Institute, The University of Melbourne, Parkville, Victoria, Australia.
Dhana G GorasiaOral Health Cooperative Research Centre, Melbourne Dental School, Bio21 Institute, The University of Melbourne, Parkville, Victoria, Australia.
Takashi TominagaDepartment of Microbiology and Oral Infection, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki, Nagasaki, Japan.
Yuko SasakiDepartment of Microbiology and Oral Infection, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki, Nagasaki, Japan.
Eric C ReynoldsOral Health Cooperative Research Centre, Melbourne Dental School, Bio21 Institute, The University of Melbourne, Parkville, Victoria, Australia.ORCID 0000-0002-6618-4856
Koji NakayamaDepartment of Microbiology and Oral Infection, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki, Nagasaki, Japan.ORCID 0000-0001-7685-0042
Mariko NaitoDepartment of Microbiology and Oral Infection, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki, Nagasaki, Japan.ORCID 0000-0003-0769-7747
Mikio ShojiDepartment of Microbiology and Oral Infection, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki, Nagasaki, Japan.ORCID 0000-0002-7605-4721

Funding

Australian National Health & Medical Research Council 1193647Japan Society for the Promotion of Science 20K09921
6 · The paper itself

Abstract

Porphyromonas gingivalis is an important bacterium associated with chronic periodontitis. The type IX secretion system (T9SS) in P. gingivalis secretes conserved C-terminal domain (CTD) containing proteins, which are also called T9SS cargo proteins, including gingipain proteinases, to the cell surface and extracellular milieu. We have shown that gene expression of some T9SS component proteins is regulated by a two-component regulatory system, PorX-PorY, an ECF sigma factor, SigP, and a T9SS cargo protein, PorA. As PorA has its own CTD, PorA is mainly localized as an A-LPS-bound form and PorV-bound form on the cell surface. However, it remains unclear how PorA can activate the PorXY-SigP signaling cascade. In this study, our results revealed that the CTD of PorA can activate the PorXY-SigP signaling cascade via interaction with PorY. It is well known that the canonical role of CTD is to act as a secretion signal for T9SS protein export. In here, we propose a novel concept that the CTD of PorA can play a dual role: as a secretion signal directing the secretion of PorA and as a positive regulator of T9SS gene expression by binding to PorY in the periplasm.

Indexed as

Bacterial ProteinsBacterial Secretion SystemsPorphyromonas gingivalisGene Expression Regulation, BacterialGingipain Cysteine EndopeptidasesLigandsSigma FactorSignal TransductionBacterial ProteinsBacterial Secretion SystemsGingipain Cysteine EndopeptidasesLigandsSigma FactorECF‐sigma factorperiodontitisPorphyromonas gingivalistwo‐component systemtype IX secretion system (T9SS)

Identifiers

PMID40195800
PMCPMC12152298

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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.