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Infection and Immunity, August 2009, p. 3294-3301, Vol. 77, No. 8
0019-9567/09/$08.00+0     doi:10.1128/IAI.00262-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Host Adhesive Activities and Virulence of Novel Fimbrial Proteins of Porphyromonas gingivalis{triangledown}

Deanne L. Pierce,1 So-ichiro Nishiyama,2,{dagger} Shuang Liang,1 Min Wang,1 Martha Triantafilou,3 Kathy Triantafilou,3 Fuminobu Yoshimura,2 Donald R. Demuth,1,4 and George Hajishengallis1,4*

Department of Periodontics/Oral Health and Systemic Disease, University of Louisville School of Dentistry, Louisville, Kentucky 40292,1 Department of Microbiology, School of Dentistry, Aichi-Gakuin University, Nagoya 464-8650, Japan,2 Infection and Immunity Group, School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9QG, United Kingdom,3 Department of Microbiology and Immunology, University of Louisville School of Medicine, Louisville, Kentucky 402924

Received 6 March 2009/ Returned for modification 15 April 2009/ Accepted 1 June 2009

The fimbriae of Porphyromonas gingivalis mediate critical roles in host colonization and evasion of innate defenses and comprise polymerized fimbrilin (FimA) associated with quantitatively minor accessory proteins (FimCDE) of unknown function. We now show that P. gingivalis fimbriae lacking FimCDE fail to interact with the CXC-chemokine receptor 4 (CXCR4), and bacteria expressing FimCDE-deficient fimbriae cannot exploit CXCR4 in vivo for promoting their persistence, as the wild-type organism does. Consistent with these loss-of-function experiments, purified FimC and FimD (but not FimE) were shown to interact with CXCR4. However, significantly stronger binding was observed when a combination of all three proteins was allowed to interact with CXCR4. In addition, FimC and FimD bound to fibronectin and type 1 collagen, whereas FimE failed to interact with these matrix proteins. These data and the fact that FimE is required for the association of FimCDE with P. gingivalis fimbriae suggest that FimE may recruit FimC and FimD into a functional complex, rather than directly binding host proteins. Consistent with this notion, FimE was shown to bind both FimC and FimD. In summary, the FimCDE components cooperate and impart critical adhesive and virulence properties to P. gingivalis fimbriae.

* Corresponding author. Mailing address: University of Louisville Health Sciences Center, 501 South Preston Street, Room 206, Louisville, KY 40292. Phone: (502) 852-5276. Fax: (502) 852-4052. E-mail: g0haji01{at}louisville.edu

{triangledown} Published ahead of print on 8 June 2009.

Editor: B. A. McCormick

{dagger} Present address: Department of Frontier Bioscience, Faculty of Bioscience and Applied Chemistry, Hosei University, 3-7-2 Kajino-cho, Koganei, Tokyo 184-8584, Japan.

Infection and Immunity, August 2009, p. 3294-3301, Vol. 77, No. 8
0019-9567/09/$08.00+0     doi:10.1128/IAI.00262-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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