This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Murakami, Y. Articles by Hanazawa, S. Search for Related Content PubMed PubMed Citation Articles by Murakami, Y. Articles by Hanazawa, S.

 Previous Article  |  Next Article 

Infect. Immun., 07 1996, 2571-2576, Vol 64, No. 7
Copyright © 1996, American Society for Microbiology

Porphyromonas gingivalis fimbrillin is one of the fibronectin-binding proteins

Y Murakami, H Iwahashi, H Yasuda, T Umemoto, I Namikawa, S Kitano and S Hanazawa
Department of Oral Microbiology, Meikai University School of Dentistry, Keyakidai, Sakado City, Saitama, Japan.

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.

This article has been cited by other articles:

• Ozaki, K., Hanazawa, S. (2001). Porphyromonas gingivalis Fimbriae Inhibit Caspase-3-Mediated Apoptosis of Monocytic THP-1 Cells under Growth Factor Deprivation via Extracellular Signal-Regulated Kinase-Dependent Expression of p21 Cip/WAF1. Infect. Immun. 69: 4944-4950 [Abstract] [Full Text]  
• Takeshita, A., Imai, K., Hanazawa, S. (1999). CpG Motifs in Porphyromonas gingivalis DNA Stimulate Interleukin-6 Expression in Human Gingival Fibroblasts. Infect. Immun. 67: 4340-4345 [Abstract] [Full Text]  
• Kontani, M., Amano, A., Nakamura, T., Nakagawa, I., Kawabata, S., Hamada, S. (1999). Inhibitory Effects of Protamines on Proteolytic and Adhesive Activities of Porphyromonas gingivalis. Infect. Immun. 67: 4917-4920 [Abstract] [Full Text]  
• Rocha, C. L., Fischetti, V. A. (1999). Identification and Characterization of a Novel Fibronectin-Binding Protein on the Surface of Group A Streptococci. Infect. Immun. 67: 2720-2728 [Abstract] [Full Text]  
• Lamont, R. J., Jenkinson, H. F. (1998). Life Below the Gum Line: Pathogenic Mechanisms of Porphyromonas gingivalis. Microbiol. Mol. Biol. Rev. 62: 1244-1263 [Abstract] [Full Text]  
• Takeshita, A., Murakami, Y., Yamashita, Y., Ishida, M., Fujisawa, S., Kitano, S., Hanazawa, S. (1998). Porphyromonas gingivalis Fimbriae Use beta 2 Integrin (CD11/CD18) on Mouse Peritoneal Macrophages as a Cellular Receptor, and the CD18 beta  Chain Plays a Functional Role in Fimbrial Signaling. Infect. Immun. 66: 4056-4060 [Abstract] [Full Text]