title: Porphyromonas gingivalis fimbrillin is one of the fibronectin-binding proteins.
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.
authors.affiliation: Department of Oral Microbiology, Meikai University School of Dentistry, Keyakidai, Sakado City, Saitama, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Murakami
authors.forename: H
authors.initials: H
authors.lastname: Iwahashi
authors.forename: H
authors.initials: H
authors.lastname: Yasuda
authors.forename: T
authors.initials: T
authors.lastname: Umemoto
authors.forename: I
authors.initials: I
authors.lastname: Namikawa
authors.forename: S
authors.initials: S
authors.lastname: Kitano
authors.forename: S
authors.initials: S
authors.lastname: Hanazawa
mesh_terms: D018829:Adhesins, Bacterial; D000328:Adult; D000818:Animals; D001422:Bacterial Adhesion / Q000502:physiology; D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D001665:Binding Sites; D002352:Carrier Proteins; D054360:Chemokine CXCL1; D019743:Chemokines, CXC; D002630:Chemotactic Factors / Q000096:biosynthesis / Q000235:genetics; D005353:Fibronectins / Q000378:metabolism*; D036781:Fimbriae Proteins; D010861:Fimbriae, Bacterial / Q000378:metabolism; D015870:Gene Expression; D006133:Growth Substances / Q000096:biosynthesis / Q000235:genetics; D006493:Heparin / Q000378:metabolism; D006801:Humans; D066298:In Vitro Techniques; D036341:Intercellular Signaling Peptides and Proteins; D007375:Interleukin-1 / Q000096:biosynthesis / Q000235:genetics; D008070:Lipopolysaccharides / Q000378:metabolism; D017737:Macrophages, Peritoneal / Q000276:immunology / Q000378:metabolism / Q000382:microbiology; D051379:Mice; D008807:Mice, Inbred BALB C; D010510:Periodontal Diseases / Q000209:etiology; D016966:Porphyromonas gingivalis / Q000378:metabolism* / Q000472:pathogenicity*; D011485:Protein Binding
chemical_list: D018829:Adhesins, Bacterial; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; C475829:CXCL1 protein, human; D002352:Carrier Proteins; D054360:Chemokine CXCL1; D019743:Chemokines, CXC; D002630:Chemotactic Factors; C475895:Cxcl1 protein, mouse; D005353:Fibronectins; D006133:Growth Substances; D036341:Intercellular Signaling Peptides and Proteins; D007375:Interleukin-1; D008070:Lipopolysaccharides; C078635:fibronectin-binding proteins, bacterial; C063055:fimbrillin; D036781:Fimbriae Proteins; D006493:Heparin