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Infection and Immunity, January 2002, p. 277-285, Vol. 70, No. 1
0019-9567/01/$04.00+0     DOI: 10.1128/IAI.70.1.277-285.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Functional Differences among FimA Variants of Porphyromonas gingivalis and Their Effects on Adhesion to and Invasion of Human Epithelial Cells

Ichiro Nakagawa,1* Atsuo Amano,2 Masae Kuboniwa,2 Takayuki Nakamura,1 Shigetada Kawabata,1 and Shigeyuki Hamada1

Departments of Oral Microbiology,1 Oral Science Methodology, Osaka University Graduate School of Dentistry, 1-8 Yamadaoka, Suita-Osaka 565-0871, Japan2

Received 22 May 2001/ Returned for modification 24 July 2001/ Accepted 3 October 2001

Fimbriae of Porphyromonas gingivalis, a periodontopathogen, play an important role in its adhesion to and invasion of host cells. The fimA genes encoding fimbrillin (FimA), a subunit protein of fimbriae, have been classified into five types, types I to V, based on nucleotide sequences. We previously reported that P. gingivalis with type II fimA was strongly associated with adult periodontitis. In the present study, we compared the abilities of recombinant FimA (rFimA) types I to V to adhere to and invade human gingival fibroblasts (HGF) and a human epithelial cell line (HEp-2 cells) by using rFimA-conjugated microspheres (rFimA-MS). There were no significant differences in the abilities of the rFimA-MS to adhere to HGF; however, the adhesion of type II rFimA-MS to HEp-2 cells was significantly greater than those of other types of rFimA-MS. We also observed that type II rFimA-MS invaded epithelial cells and accumulated around the nuclei. These adhesion and invasion characteristics were eliminated by the addition of antibodies to type II rFimA and {alpha}5ß1-integrin. In contrast, Arg-Gly-Asp-Ser peptide and a synthetic peptide of proline-rich protein C had negligible inhibitory effects. Furthermore, P. gingivalis strain HW24D1 with type II fimA adhered to cells and invaded them more than strains with other fimA genotypes. These results suggest that type II FimA can bind to epithelial cells most efficiently through specific host receptors.

* Corresponding author. Mailing address: Department of Oral Microbiology, Osaka University Graduate School of Dentistry, 1-8 Yamadaoka, Suita-Osaka 565-0871, Japan. Phone: 81-6-6879-2897. Fax: 81-6-6878-4755. E-mail: ichiro{at}dent.osaka-u.ac.jp.

Editor: V. J. DiRita

Infection and Immunity, January 2002, p. 277-285, Vol. 70, No. 1
0019-9567/01/$04.00+0     DOI: 10.1128/IAI.70.1.277-285.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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