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Porphyromonas gingivalis as a Model Organism for Assessing Interaction of Anaerobic Bacteria with Host Cells
12:16

Porphyromonas gingivalis as a Model Organism for Assessing Interaction of Anaerobic Bacteria with Host Cells

Published on: December 17, 2015

Role of vimA in cell surface biogenesis in Porphyromonas gingivalis

Devon O Osbourne1, Wilson Aruni1, Francis Roy1

  • 1Division of Microbiology and Molecular Genetics, School of Medicine, Loma Linda University, Loma Linda, CA 92350, USA.

Microbiology (Reading, England)
|April 10, 2010
PubMed

Insights

The Porphyromonas gingivalis vimA gene is crucial for cell surface protein biogenesis. A vimA-defective mutant showed altered fimbriae, capsule, and outer membrane proteins, impacting cell surface characteristics.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Cell Biology

Background:

  • The Porphyromonas gingivalis vimA gene is implicated in gingipain biogenesis.
  • A vimA-defective mutant (FLL92) exhibits increased auto-aggregation, suggesting altered membrane surface proteins.

Purpose of the Study:

  • To elucidate the role of the VimA protein in P. gingivalis cell surface biogenesis.
  • To characterize the surface morphology and protein composition of a vimA-defective mutant.

Main Methods:

  • Transmission electron microscopy (TEM) and atomic force microscopy (AFM) for surface morphology.
  • Western blot analysis with anti-FimA antibodies.
  • Antibiotic sensitivity testing (globomycin, vancomycin).
  • Lectin-binding assays and proteomic analysis of outer membrane fractions.

Main Results:

  • TEM revealed abundant fimbriae and an irregular capsule in the FLL92 mutant compared to wild-type.
  • AFM showed a rougher surface in FLL92. A 41 kDa FimA-related protein was detected in FLL92 but not wild-type.
  • FLL92 displayed increased sensitivity to globomycin and vancomycin, with altered outer membrane protein profiles including differential presence/absence of 29 proteins.

Conclusions:

  • VimA influences capsular synthesis and fimbrial expression in P. gingivalis.
  • VimA plays a role in the glycosylation and anchoring of multiple surface proteins.
  • These alterations in cell surface characteristics likely contribute to the observed phenotypes in vimA-defective mutants.

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