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.

Plos One
|March 16, 2017
PubMed

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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