ArticleInternational journal of molecular medicine2019
Recombinant fimbriae protein of Porphyromonas gingivalis induces an inflammatory response via the TLR4/NF‑κB signaling pathway in human peripheral blood mononuclear cells.
Article in International journal of molecular medicine, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 16 citations in OpenAlex.
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- Multifunctional role of oral bacteria in the progression of non-alcoholic fatty liver disease.World journal of hepatology · 2024Review
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- Identification of bio-active secondary metabolites from Actinobacteria as potential drug targets againstIn silico pharmacology · 2024Article
- The oral-gut-circulatory axis: from homeostasis to colon cancer.Frontiers in cellular and infection microbiology · 2023Review
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- Oral and Gut Microbial Dysbiosis and Non-alcoholic Fatty Liver Disease: The Central Role ofFrontiers in medicine · 2022Review
- Periodontitis Exacerbates and Promotes the Progression of Chronic Kidney Disease Through Oral Flora, Cytokines, and Oxidative Stress.Frontiers in microbiology · 2021Review
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- Triticum vulgare Extract Modulates Protein-Kinase B and Matrix Metalloproteinases 9 Protein Expression in BV-2 Cells: Bioactivity on Inflammatory Pathway Associated with Molecular Mechanism Wound Healing.Mediators of inflammation · 2020Article
- Nasal double DNA adjuvant induces salivary FimA-specific secretory IgA antibodies in young and aging mice and blocks Porphyromonas gingivalis binding to a salivary protein.BMC oral health · 2019Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Porphyromonas gingivalis (P. gingivalis) is a periodontal pathogen that may accumulate with other organisms in subgingival plaque biofilms and is associated with periodontal disease. P. gingivalis fimbriae (FimA) is a filamentous structure on the surface of bacteria that is closely associated with bacterial adhesion to and colonization of host tissues, and serves an essential role in biofilm formation. The present study aimed to construct P. gingivalis FimA prokaryotic expression plasmids, purify a FimA fusion protein and explore the effect of a recombinant FimA protein on the inflammatory response in human peripheral blood mononuclear cells (PBMCs). P. gingivalis FimA prokaryotic expression plasmids were constructed by gene cloning and recombination technology. SDS‑PAGE was used to evaluate the purified recombinant FimA protein. The cell proliferation rate and inflammatory cytokine expression of PBMCs treated with the FimA fusion protein with or without transfection with toll‑like receptor 4 (TLR4) small interfering (si)RNA were detected by CCK‑8 assays and ELISAs, respectively. The expression levels of TLR4, nuclear factor kappa‑light‑chain‑enhancer of activated B cells (NF‑κB) and myeloid differentiation primary response 88 (MyD88) in PBMCs were detected by western blot analysis and reverse transcription quantitative polymerase chain reaction. A FimA fusion protein with high purity was obtained. FimA fusion protein treatment significantly increased PBMC proliferation and promoted the release of tumor necrosis factor‑α (TNF‑α), interleukin (IL)‑6, matrix metalloproteinase (MMP)‑8 and MMP‑9 in PBMCs. TLR4 interference reversed the effects of the FimA fusion protein on PBMC proliferation and inflammatory cytokine release. The expression levels of TLR4, NF‑κB and MyD88 in PBMCs were significantly increased following treatment with the FimA fusion protein, while the expression levels of these genes at the mRNA and protein levels decreased significantly in PBMCs following FimA fusion protein treatment and TLR4 interference. The FimA fusion protein increased PBMC proliferation and promoted the release of the inflammatory cytokines TNF‑α, IL‑6, MMP‑8 and MMP‑9 via the TLR4/NF‑κB signaling pathway. FimA may serve as a promising therapeutic strategy for periodontal disease.
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