Evidence map›Paper›PMID 41813854›Full record

ArticleScientific reports2026

Nisin bacteriocin blocks T. denticola-triggered MMP2 activation and pathogen internalization via TLR2.

Pachiyappan Kamarajan, Allan Radaic, Hossein Beheshti, Mishri Parikh, Sarah Lo, J Christopher Fenno, Yvonne L Hernandez Kapila

Abstract read
In one paragraph

Article in Scientific reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

7 authors.

Pachiyappan KamarajanDepartment of Biosystems and Function, School of Dentistry, University of California Los Angeles, Los Angeles, CA, USA.
Allan RadaicDepartment of Biosystems and Function, School of Dentistry, University of California Los Angeles, Los Angeles, CA, USA.
Hossein BeheshtiDepartment of Biosystems and Function, School of Dentistry, University of California Los Angeles, Los Angeles, CA, USA.
Mishri ParikhDepartment of Biosystems and Function, School of Dentistry, University of California Los Angeles, Los Angeles, CA, USA.
Sarah LoDepartment of Biosystems and Function, School of Dentistry, University of California Los Angeles, Los Angeles, CA, USA.
J Christopher FennoDepartment of Biologic and Materials Sciences & Prosthodontics, School of Dentistry, University of Michigan, Ann Arbor, MI, USA.
Yvonne L Hernandez KapilaDepartment of Biosystems and Function, School of Dentistry, University of California Los Angeles, Los Angeles, CA, USA. ykapila@dentistry.ucla.edu.

Funding

Treponema - Host Cell and Tissue InteractionsR01DE025225 · NIDCR · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI J CHRISTOPHER FENNO, Yvonne L Kapila · 2015 to 2026
$6.3M
Surface protein complexes of oral treponemes: assembly and host cell interactionsR01DE018221 · NIDCR · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI FENNO, J CHRISTOPHER · 2009 to 2010
$752k
NIDCR NIH HHS R01 DE018221NIDCR NIH HHS R01 DE025225
6 · The paper itself

Abstract

We examined Treponema denticola-induced dysregulation of toll-like receptor (TLR) signaling and its downstream effects on matrix metalloproteinase 2 (MMP2) expression and activation in periodontal cells, and whether the antimicrobial peptide nisin could modulate this process. T. denticola and its outer membrane protease dentilisin/PrtP activated MMP2, whereas a dentilisin/PrtP-deficient T. denticola mutant did not, and nisin attenuated this response. Dentilisin/PrtP directly activated recombinant MMP2 in vitro. T. denticola-mediated MMP2 activation was TLR2-dependent, since TLR2 suppression abrogated MMP2 activation, reduced MMP2 mRNA expression, and reduced T. denticola internalization. Nisin significantly inhibited T. denticola internalization. Computational modeling suggests dentilisin/PrtP directly binds pro-MMP2, whereas nisin binds dentilisin/PrtP but not pro-MMP2. Thus, nisin may interfere with MMP2 activation by binding to dentilisin/PrtP. These findings reveal a novel mechanism by which T. denticola and nisin regulate MMP2, and underscore nisin’s potential as a therapeutic for modulating bacterial-mediated tissue damage during periodontal disease.

Indexed as

Matrix Metalloproteinase 2NisinToll-Like Receptor 2Treponema denticolaAntimicrobial PeptidesBacterial ProteinsEnzyme ActivationEnzyme PrecursorsHumansPeptide HydrolasesSignal TransductionAntimicrobial PeptidesBacterial ProteinsdentilisinEnzyme PrecursorsMatrix Metalloproteinase 2NisinPeptide HydrolasesTLR2 protein, humanToll-Like Receptor 2Antimicrobial peptideDentilisin/PrtPMatrix metalloproteinases 2 proteinNisinPeriodontal ligament cellsPrtPToll-like receptor-2Treponema denticola

Identifiers

PMID41813854
PMCPMC13100033

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.