Skip to main content
PMC home page
Infection and Immunity logoLink to Infection and Immunity
. 1997 Feb;65(2):815–817. doi: 10.1128/iai.65.2.815-817.1997

Porphyromonas gingivalis fimbria-stimulated bone resorption is inhibited through binding of the fimbriae to fibronectin.

Y Kawata 1, H Iwasaka 1, S Kitano 1, S Hanazawa 1
PMCID: PMC176132  PMID: 9009349

Abstract

Our most recent study demonstrated that fibronectin is one of the Porphyromonas gingivalis fimbria-binding proteins. In this present study, we demonstrate with mouse embryonic calvarial cells that P. gingivalis fimbria-stimulated bone resorption is inhibited by human fibronectin. The fibronectin inhibition was dose and culture time dependent and was completely neutralized by antifibronectin antibody. The inhibitory action of fibronectin depended on fimbrial interaction with the heparin-binding and cell-attachment domains in the fibronectin structure.

Full Text

The Full Text of this article is available as a PDF (188.5 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Amano S., Hanazawa S., Kawata Y., Ohta K., Kitami H., Kitano S. An assay system utilizing devitalized bone for assessment of differentiation of osteoclast progenitors. J Bone Miner Res. 1992 Mar;7(3):321–328. doi: 10.1002/jbmr.5650070312. [DOI] [PubMed] [Google Scholar]
  2. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  3. Evans R. T., Klausen B., Genco R. J. Immunization with fimbrial protein and peptide protects against Porphyromonas gingivalis-induced periodontal tissue destruction. Adv Exp Med Biol. 1992;327:255–262. doi: 10.1007/978-1-4615-3410-5_27. [DOI] [PubMed] [Google Scholar]
  4. Evans R. T., Klausen B., Sojar H. T., Bedi G. S., Sfintescu C., Ramamurthy N. S., Golub L. M., Genco R. J. Immunization with Porphyromonas (Bacteroides) gingivalis fimbriae protects against periodontal destruction. Infect Immun. 1992 Jul;60(7):2926–2935. doi: 10.1128/iai.60.7.2926-2935.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Hanazawa S., Hirose K., Ohmori Y., Amano S., Kitano S. Bacteroides gingivalis fimbriae stimulate production of thymocyte-activating factor by human gingival fibroblasts. Infect Immun. 1988 Jan;56(1):272–274. doi: 10.1128/iai.56.1.272-274.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Hanazawa S., Murakami Y., Takeshita A., Kitami H., Ohta K., Amano S., Kitano S. Porphyromonas gingivalis fimbriae induce expression of the neutrophil chemotactic factor KC gene of mouse peritoneal macrophages: role of protein kinase C. Infect Immun. 1992 Apr;60(4):1544–1549. doi: 10.1128/iai.60.4.1544-1549.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hanazawa S., Murakami Y., Takeshita A., Kitami H., Ohta K., Amano S., Kitano S. Porphyromonas gingivalis fimbriae induce expression of the neutrophil chemotactic factor KC gene of mouse peritoneal macrophages: role of protein kinase C. Infect Immun. 1992 Apr;60(4):1544–1549. doi: 10.1128/iai.60.4.1544-1549.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hook M., McGavin M. J., Switalski L. M., Raja R., Raucci G., Lindgren P. E., Lindberg M., Signas C. Interactions of bacteria with extracellular matrix proteins. Cell Differ Dev. 1990 Dec 2;32(3):433–438. doi: 10.1016/0922-3371(90)90060-a. [DOI] [PubMed] [Google Scholar]
  9. Isogai E., Hirose K., Fujii N., Isogai H. Three types of binding by Porphyromonas gingivalis and oral bacteria to fibronectin, buccal epithelial cells and erythrocytes. Arch Oral Biol. 1992 Aug;37(8):667–670. doi: 10.1016/0003-9969(92)90130-z. [DOI] [PubMed] [Google Scholar]
  10. Kawata Y., Hanazawa S., Amano S., Murakami Y., Matsumoto T., Nishida K., Kitano S. Porphyromonas gingivalis fimbriae stimulate bone resorption in vitro. Infect Immun. 1994 Jul;62(7):3012–3016. doi: 10.1128/iai.62.7.3012-3016.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Kukkonen M., Raunio T., Virkola R., Lähteenmäki K., Mäkelä P. H., Klemm P., Clegg S., Korhonen T. K. Basement membrane carbohydrate as a target for bacterial adhesion: binding of type I fimbriae of Salmonella enterica and Escherichia coli to laminin. Mol Microbiol. 1993 Jan;7(2):229–237. doi: 10.1111/j.1365-2958.1993.tb01114.x. [DOI] [PubMed] [Google Scholar]
  12. Lantz M. S., Allen R. D., Duck L. W., Blume J. L., Switalski L. M., Hook M. Identification of Porphyromonas gingivalis components that mediate its interactions with fibronectin. J Bacteriol. 1991 Jul;173(14):4263–4270. doi: 10.1128/jb.173.14.4263-4270.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Ljungh A., Emödy L., Steinruck H., Sullivan P., West B., Zetterberg E., Wadström T. Fibronectin, vitronectin, and collagen binding to Escherichia coli of intestinal and extraintestinal origin. Zentralbl Bakteriol. 1990 Oct;274(1):126–134. doi: 10.1016/s0934-8840(11)80982-5. [DOI] [PubMed] [Google Scholar]
  14. Murakami Y., Iwahashi H., Yasuda H., Umemoto T., Namikawa I., Kitano S., Hanazawa S. Porphyromonas gingivalis fimbrillin is one of the fibronectin-binding proteins. Infect Immun. 1996 Jul;64(7):2571–2576. doi: 10.1128/iai.64.7.2571-2576.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Naito Y., Gibbons R. J. Attachment of Bacteroides gingivalis to collagenous substrata. J Dent Res. 1988 Aug;67(8):1075–1080. doi: 10.1177/00220345880670080301. [DOI] [PubMed] [Google Scholar]
  16. Obara M., Kang M. S., Rocher-Dufour S., Kornblihtt A., Thiery J. P., Yamada K. M. Expression of the cell-binding domain of human fibronectin in E. coli. Identification of sequences promoting full to minimal adhesive function. FEBS Lett. 1987 Mar 23;213(2):261–264. doi: 10.1016/0014-5793(87)81502-8. [DOI] [PubMed] [Google Scholar]
  17. Sojar H. T., Lee J. Y., Genco R. J. Fibronectin binding domain of P. gingivalis fimbriae. Biochem Biophys Res Commun. 1995 Nov 22;216(3):785–792. doi: 10.1006/bbrc.1995.2690. [DOI] [PubMed] [Google Scholar]
  18. Steiner B. M., Sell S., Schell R. F. Treponema pallidum attachment to surface and matrix proteins of cultured rabbit epithelial cells. J Infect Dis. 1987 Apr;155(4):742–748. doi: 10.1093/infdis/155.4.742. [DOI] [PubMed] [Google Scholar]
  19. Switalski L. M., Murchison H., Timpl R., Curtiss R., 3rd, Hök M. Binding of laminin to oral and endocarditis strains of viridans streptococci. J Bacteriol. 1987 Mar;169(3):1095–1101. doi: 10.1128/jb.169.3.1095-1101.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Talay S. R., Valentin-Weigand P., Jerlström P. G., Timmis K. N., Chhatwal G. S. Fibronectin-binding protein of Streptococcus pyogenes: sequence of the binding domain involved in adherence of streptococci to epithelial cells. Infect Immun. 1992 Sep;60(9):3837–3844. doi: 10.1128/iai.60.9.3837-3844.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Umemoto T., Namikawa I. Binding of host-associated treponeme proteins to collagens and laminin: a possible mechanism of spirochetal adherence to host tissues. Microbiol Immunol. 1994;38(8):655–663. doi: 10.1111/j.1348-0421.1994.tb01836.x. [DOI] [PubMed] [Google Scholar]
  22. Visai L., Speziale P., Bozzini S. Binding of collagens to an enterotoxigenic strain of Escherichia coli. Infect Immun. 1990 Feb;58(2):449–455. doi: 10.1128/iai.58.2.449-455.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Winkler J. R., John S. R., Kramer R. H., Hoover C. I., Murray P. A. Attachment of oral bacteria to a basement-membrane-like matrix and to purified matrix proteins. Infect Immun. 1987 Nov;55(11):2721–2726. doi: 10.1128/iai.55.11.2721-2726.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Yoshimura F., Takahashi K., Nodasaka Y., Suzuki T. Purification and characterization of a novel type of fimbriae from the oral anaerobe Bacteroides gingivalis. J Bacteriol. 1984 Dec;160(3):949–957. doi: 10.1128/jb.160.3.949-957.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Infection and Immunity are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES