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Infection and Immunity, April 2005, p. 2157-2163, Vol. 73, No. 4
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.4.2157-2163.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Lipopolysaccharide Preparation Extracted from Porphyromonas gingivalis Lipoprotein-Deficient Mutant Shows a Marked Decrease in Toll-Like Receptor 2-Mediated Signaling

Yasuyuki Asai,1 Masahito Hashimoto,1 Hansel M. Fletcher,2 Kensuke Miyake,3 Shizuo Akira,4 and Tomohiko Ogawa1*

Department of Oral Microbiology, Asahi University School of Dentistry, Gifu,1 Division of Infectious Genetics, Department of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, Tokyo,3 Department of Host Defense, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan,4 Division of Microbiology and Molecular Genetics, School of Medicine, Loma Linda University, Loma Linda, California2

Received 8 October 2004/ Returned for modification 11 November 2004/ Accepted 8 December 2004

We recently demonstrated that a new PG1828-encoded lipoprotein (PG1828LP) was able to be separated from a Porphyromonas gingivalis lipopolysaccharide (LPS) preparation, and we found that it exhibited strong cell activation, similar to that of Escherichia coli LPS, through a Toll-like receptor 2 (TLR2)-dependent pathway. In order to determine the virulence of PG1828LP toward cell activation, we generated a PG1828-deficient mutant of P. gingivalis strain 381 by allelic exchange mutagenesis using an ermF-ermAM antibiotic resistance cassette. A highly purified preparation of LPS from a PG1828-deficient mutant ({Delta}PG1828-LPS) showed nearly the same ladder-like patterns in silver-stained gels as a preparation of LPS from a wild-type strain (WT-LPS), as well as Limulus amoebocyte lysate activities that were similar to those of the WT-LPS preparation. However, the ability of the {Delta}PG1828-LPS preparation to activate NF-{kappa}B in TLR2-expressing cells was markedly attenuated. Cytokine production by human gingival fibroblasts was also decreased in response to the {Delta}PG1828-LPS preparation in comparison with the WT-LPS preparation, and the activity was comparable to the stimulation of highly purified lipid A of P. gingivalis by TLR4. Further, lethal toxicity was rarely observed following intraperitoneal injection of the PG1828-deficient mutant into mice compared to that with the wild-type strain, while the {Delta}PG1828-LPS preparation showed no lethal toxicity. Taken together, these results clearly indicate that PG1828LP plays an essential role in inflammatory responses and may be a major virulence factor of P. gingivalis.

* Corresponding author. Mailing address: Department of Oral Microbiology, Asahi University School of Dentistry, 1851-1 Hozumi, Mizuho, Gifu 501-0296, Japan. Phone: 81-58-329-1421. Fax: 81-58-329-1421. E-mail: tomo527{at}dent.asahi-u.ac.jp.

Editor: W. A. Petri, Jr.

Infection and Immunity, April 2005, p. 2157-2163, Vol. 73, No. 4
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.4.2157-2163.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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