Evidence map›Paper›PMID 41261887›Full record

ArticleMicrobiology and immunology2026

OmpA_C-Like Domain of PorE Is Essential for PorE Function in the Type IX Secretion System (T9SS) of Porphyromonas gingivalis and Some T9SS Cargo Proteins Are Secreted in a PorE-Independent Manner.

Takashi Tominaga, Hideharu Yukitake, Paul D Veith, Dhana G Gorasia, Takao Ayuse, Takuro Sanuki, Eric C Reynolds, Koji Nakayama, Mariko Naito, Mikio Shoji

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Microbiology and immunology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

10 authors.

Takashi TominagaDepartment of Microbiology and Oral Infection, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki, Japan.
Hideharu YukitakeDepartment of Microbiology and Oral Infection, Graduate School of Biomedical Sciences, Nagasaki University, 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.
Takao AyuseDepartment of Clinical Physiology, Nagasaki University Graduate School of Biomedical Sciences, Nagasaki, Japan.
Takuro SanukiDepartment of Clinical Physiology, Nagasaki University Graduate School of Biomedical Sciences, Nagasaki, Japan.ORCID https://orcid.org/0000-0002-1347-2627
Eric C ReynoldsOral Health Cooperative Research Centre, Melbourne Dental School, Bio21 Institute, The University of Melbourne, Parkville, Victoria, Australia.ORCID https://orcid.org/0000-0002-6618-4856
Koji NakayamaDepartment of Microbiology and Oral Infection, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki, Japan.ORCID https://orcid.org/0000-0001-7685-0042
Mariko NaitoDepartment of Microbiology and Oral Infection, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki, Japan.ORCID https://orcid.org/0000-0003-0769-7747
Mikio ShojiDepartment of Microbiology and Oral Infection, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki, Japan.ORCID https://orcid.org/0000-0002-7605-4721

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The periodontal pathogen Porphyromonas gingivalis secretes gingipains, highly hydrolytic proteases, to the cell surface or external environment via a type IX secretion system (T9SS). PorE is one of the T9SS component proteins essential for gingipain secretion. It consists of four domains: TPR, WD40, CRD, and OmpA_C-like. In this study, we investigated the contribution and function of these PorE domains to gingipain secretion by generating PorE mutants with domain deletions and residue substitutions. We found that (i) the OmpA_C-like domain is essential for gingipain secretion, (ii) the peptidoglycan binding sites (Asp

Indexed as

Adhesins, BacterialBacterial Outer Membrane ProteinsBacterial ProteinsBacterial Secretion SystemsCysteine EndopeptidasesPorphyromonas gingivalisGingipain Cysteine EndopeptidasesPeptidoglycanProtein DomainsProtein TransportAdhesins, BacterialBacterial Outer Membrane ProteinsBacterial ProteinsBacterial Secretion SystemsCysteine EndopeptidasesGingipain Cysteine EndopeptidasesPeptidoglycanperiodontitisPorphyromonas gingivalistype IX secretion system (T9SS)

Identifiers

PMID41261887
PMCPMC12773672

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.