ArticleInfection and immunity2010
Tetratricopeptide repeat protein-associated proteins contribute to the virulence of Porphyromonas gingivalis.
Article in Infection and immunity, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 55 citations in OpenAlex.
- Virulence diversity amongJournal of oral microbiology · 2026Review
- PorA of the Type IX Secretion Is a Ligand of the PorXY Two-Component Regulatory System in Porphyromonas gingivalis.Molecular microbiology · 2025Article
- Outer Membrane Vesicles Derived From Fusobacterium nucleatum Trigger Periodontitis Through Host Overimmunity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Illuminating the oral microbiome and its host interactions: tools and approaches for molecular microbiology studies.FEMS microbiology reviews · 2023Review
- Hemin availability induces coordinated DNA methylation and gene expression changes inmSystems · 2023Article
- Comparative Genomics Reveals Evolutionary Traits, Mating Strategies, and Pathogenicity-Related Genes Variation ofFrontiers in microbiology · 2022Article
- Polymicrobial synergy stimulates Porphyromonas gingivalis survival and gingipain expression in a multi-species subgingival community.BMC oral health · 2021Article
- PorA, a conserved C-terminal domain-containing protein, impacts the PorXY-SigP signaling of the type IX secretion system.Scientific reports · 2020Article
- 101Studies in mycology · 2020Article
- Functional Annotation and Curation of Hypothetical Proteins Present in A Newly Emerged Serotype 1c ofGenes · 2020Article
- Article
- Transcriptome analysis of Porphyromonas gingivalis and Acinetobacter baumannii in polymicrobial communities.Molecular oral microbiology · 2018Article
- Rv0613c/MSMEG_1285 Interacts with HBHA and Mediates Its Proper Cell-Surface Exposure in Mycobacteria.International journal of molecular sciences · 2018Article
- [Research progress on the type Ⅸ secretion system of Porphyromonas gingivalis].Hua xi kou qiang yi xue za zhi = Huaxi kouqiang yixue zazhi = West China journal of stomatology · 2017Article
- The Type IX Secretion System (T9SS): Highlights and Recent Insights into Its Structure and Function.Frontiers in cellular and infection microbiology · 2017Review
- Article
- Genes Contributing toFrontiers in cellular and infection microbiology · 2017Article
- Insights into Dynamic Polymicrobial Synergy Revealed by Time-Coursed RNA-Seq.Frontiers in microbiology · 2017Article
- Structure of RagB, a major immunodominant outer-membrane surface receptor antigen of Porphyromonas gingivalis.Molecular oral microbiology · 2016Article
- Involvement of an Skp-Like Protein, PGN_0300, in the Type IX Secretion System of Porphyromonas gingivalis.Infection and immunity · 2016Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Porphyromonas gingivalis is one of the most etiologically important microorganisms in periodontal disease. We found in a previous study that PG1385 (TprA) protein, a tetratricopeptide repeat (TPR) protein, was upregulated in P. gingivalis wild-type cells placed in a mouse subcutaneous chamber and that a tprA mutant was clearly less virulent in the mouse subcutaneous abscess model (M. Yoshimura et al., Oral Microbiol. Immunol. 23:413-418, 2008). In the present study, we investigated the gene expression profile of tprA mutant cells placed in a mouse subcutaneous chamber and found that 9 genes, including PG2102 (tapA), PG2101 (tapB), and PG2100 (tapC) genes, were downregulated in the tprA mutant compared with those in the wild type. Expression of a cluster of tapA, tapB, and tapC genes of the mutant was also downregulated in an in vitro culture with enriched brain heart infusion medium. The TprA protein has three TPR motifs known as a protein-protein interaction module. Yeast two-hybrid system analysis and in vitro protein binding assays with immunoprecipitation and surface plasmon resonance detection revealed that the TprA protein could bind to TapA and TapB proteins. TprA and TapB proteins were located in the periplasmic space, whereas TapA, which appeared to be one of the C-terminal domain family proteins, was located at the outer membrane. We constructed tapA, tapB, and tapC single mutants and a tapA-tapB-tapC deletion mutant. In the mouse subcutaneous infection experiment, all of the mutants were less virulent than the wild type. These results suggest that TprA, TapA, TapB, and TapC are cooperatively involved in P. gingivalis virulence.
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