Porphyromonas gingivalis fimbrillin is one of the fibronectin-binding proteins

Infect Immun. 1996 Jul;64(7):2571-6. doi: 10.1128/iai.64.7.2571-2576.1996.

Abstract

In this study, we demonstrate that Porphyromonas gingivalis fimbrillin, a major component of bacterial fimbriae, is one of the fibronectin-binding proteins and that fibronectin is a potent inhibitor of the adherence of the bacteria to host cells and of the pathogenesis of the bacterium that acts by binding to the fimbriae. A Western blotting (immunoblotting) assay showed that fibronectin binds strongly to P. gingivalis fimbrillin. The fimbrial binding to fibronectin was also evidenced by a binding assay involving 125I-labeled fimbriae. Furthermore, fibronectin markedly inhibited the fimbria-induced expression of interleukin-1beta and neutrophil-specific chemoattractant KC genes in macrophages. The inhibitory action depended on the fimbrial interaction with heparin-binding and cell attachment domains in the fibronectin structure. The binding of P.gingivalis to mouse peritoneal macrophages via its fimbriae was inhibited by fibronectin. Fibronectin also inhibited the bacterial cell-induced expression of interleukin-1beta and KC genes in the macrophages. These results demonstrate the importance of fibronectin as a modulator of the pathogenic mechanism of P. gingivalis, a pathogen that causes adult periodontal disease.

MeSH terms

  • Adhesins, Bacterial*
  • Adult
  • Animals
  • Bacterial Adhesion / physiology
  • Bacterial Outer Membrane Proteins / metabolism*
  • Bacterial Proteins / metabolism*
  • Binding Sites
  • Carrier Proteins*
  • Chemokine CXCL1
  • Chemokines, CXC*
  • Chemotactic Factors / biosynthesis
  • Chemotactic Factors / genetics
  • Fibronectins / metabolism*
  • Fimbriae Proteins*
  • Fimbriae, Bacterial / metabolism
  • Gene Expression
  • Growth Substances / biosynthesis
  • Growth Substances / genetics
  • Heparin / metabolism
  • Humans
  • In Vitro Techniques
  • Intercellular Signaling Peptides and Proteins*
  • Interleukin-1 / biosynthesis
  • Interleukin-1 / genetics
  • Lipopolysaccharides / metabolism
  • Macrophages, Peritoneal / immunology
  • Macrophages, Peritoneal / metabolism
  • Macrophages, Peritoneal / microbiology
  • Mice
  • Mice, Inbred BALB C
  • Periodontal Diseases / etiology
  • Porphyromonas gingivalis / metabolism*
  • Porphyromonas gingivalis / pathogenicity*
  • Protein Binding

Substances

  • Adhesins, Bacterial
  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • CXCL1 protein, human
  • Carrier Proteins
  • Chemokine CXCL1
  • Chemokines, CXC
  • Chemotactic Factors
  • Cxcl1 protein, mouse
  • Fibronectins
  • Growth Substances
  • Intercellular Signaling Peptides and Proteins
  • Interleukin-1
  • Lipopolysaccharides
  • fibronectin-binding proteins, bacterial
  • fimbrillin
  • Fimbriae Proteins
  • Heparin