Reduced fimbria-associated activities of Porphyromonas gingivalis induced by recombinant fimbrial expression

FEMS Microbiol Lett. 2001 Feb 20;195(2):217-22. doi: 10.1111/j.1574-6968.2001.tb10524.x.

Abstract

The adhesion properties of the recombinant fimbriae (r-fimbriae) recovered from a YH522 transformant of Porphyromonas gingivalis which harbors a chimeric plasmid, pYHF2, containing the fimA gene of strain 381 were compared with those of the endogenous fimA fimbriae of strain 33277. The adhesion level of the r-fimbriae to Actinomyces viscosus was clearly lower than that of the endogenous fimbriae. In addition, the r-fimbriae were shown to lack some minor components detectable in the endogenous fimbriae. The plasmid pYHF2 prepared from the YH522 transformant was then transformed into six different P. gingivalis strains and the resultant pYHF2-containing strains were examined for their fimbrial expression. In spite of the presence of a considerable diversity in the expression level of the r-fimbriae among these transformants, it was evident that the strains expressing higher levels of the r-fimbriae exhibited a greater decrease in adhesion activity to other bacteria and to oral epithelial cells, as well as in self-aggregation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actinomyces viscosus / physiology
  • Bacterial Adhesion*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / physiology*
  • Cells, Cultured
  • Epithelial Cells / microbiology
  • Fimbriae Proteins*
  • Fimbriae, Bacterial / genetics
  • Fimbriae, Bacterial / physiology*
  • Gingiva / cytology
  • Gingiva / microbiology*
  • Hemagglutination
  • Humans
  • Plasmids
  • Porphyromonas gingivalis / genetics
  • Porphyromonas gingivalis / physiology*
  • Transformation, Bacterial
  • Tumor Cells, Cultured

Substances

  • Bacterial Proteins
  • fimbrillin
  • Fimbriae Proteins