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Updated: Mar 6, 2026

Porphyromonas gingivalis as a Model Organism for Assessing Interaction of Anaerobic Bacteria with Host Cells
Published on: December 17, 2015
Novel fimbrilin PGN_1808 in Porphyromonas gingivalis
Keiji Nagano1, Yoshiaki Hasegawa1, Yasuo Yoshida1
1Department of Microbiology, School of Dentistry, Aichi Gakuin University 1-100 Kusumoto-cho, Chikusa-ku, Nagoya, Aichi, Japan.
Abstract:
Porphyromonas gingivalis, a periodontopathic gram-negative anaerobic bacterium, generally expresses two types of fimbriae, FimA and Mfa1. However, a novel potential fimbrilin, PGN_1808, in P. gingivalis strain ATCC 33277 was recently identified by an in silico structural homology search. In this study, we experimentally examined whether the protein formed a fimbrial structure. Anion-exchange chromatography showed that the elution peak of the protein was not identical to those of the major fimbrilins of FimA and Mfa1, indicating that PGN_1808 is not a component of these fimbriae. Electrophoretic analyses showed that PGN_1808 formed a polymer, although it was detergent and heat labile compared to FimA and Mfa1. Transmission electron microscopy showed filamentous structures (2‒3 nm × 200‒400 nm) on the cell surfaces of a PGN_1808-overexpressing P. gingivalis mutant (deficient in both FimA and Mfa1 fimbriae) and in the PGN_1808 fraction. PGN_1808 was detected in 81 of 84 wild-type strains of P. gingivalis by western blotting, suggesting that the protein is generally present in P. gingivalis.
Insights
Researchers discovered a new fimbrial structure, PGN_1808, in Porphyromonas gingivalis. This protein forms filamentous structures and is present in most wild-type strains, distinct from known FimA and Mfa1 fimbriae.
Area of Science:
- Microbiology
- Bacteriology
- Structural Biology
Background:
- Porphyromonas gingivalis is a key pathogen in periodontitis.
- It typically expresses FimA and Mfa1 fimbriae, crucial for virulence.
- A novel protein, PGN_1808, was identified computationally as a potential fimbilin.
Purpose of the Study:
- To experimentally verify if PGN_1808 forms a fimbrial structure.
- To determine if PGN_1808 is associated with known fimbriae (FimA, Mfa1).
- To assess the prevalence of PGN_1808 in P. gingivalis strains.
Main Methods:
- Anion-exchange chromatography to separate proteins.
- Electrophoretic analysis to assess polymerization.
- Transmission electron microscopy (TEM) for structural visualization.
- Western blotting to detect PGN_1808 presence.
Main Results:
- PGN_1808 eluted separately from FimA and Mfa1, indicating it's a distinct component.
- PGN_1808 formed a polymer, though it was detergent and heat labile.
- TEM confirmed filamentous structures of PGN_1808 on bacterial surfaces.
- PGN_1808 was detected in 81% of tested P. gingivalis strains.
Conclusions:
- PGN_1808 represents a novel, independently formed fimbrial structure in P. gingivalis.
- This protein is widely distributed among P. gingivalis strains.
- PGN_1808's role in P. gingivalis pathogenesis warrants further investigation.
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