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International Immunology, Vol. 14, No. 11, pp. 1325-1332, November 2002
© 2002 Japanese Society for Immunology

Cell activation by Porphyromonas gingivalis lipid A molecule through Toll-like receptor 4- and myeloid differentiation factor 88-dependent signaling pathway

Tomohiko Ogawa1, Yasuyuki Asai1, Masahito Hashimoto1, Osamu Takeuchi2, Tomoko Kurita3, Yasunobu Yoshikai4, Kensuke Miyake5 and Shizuo Akira2

1 Department of Oral Microbiology, Asahi University School of Dentistry, 1851 Hozumi, Hozumi-Cho, Motosu-Gun, Gifu 501-0296, Japan 2 Department of Host Defense, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan 3 Department of Microbiology, Nihon University School of Dentistry at Matsudo, Chiba 271-8587, Japan 4 Division of Host Defense, Research Center for Prevention of Infectious Diseases, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan 5 Division of Infectious Genetics, Department of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, Tokyo 108-8639, Japan

Correspondence to: T. Ogawa; E-mail: tomo527{at}dent.asahi-u.ac.jp
Transmitting editor: K. Sugamura

Porphyromonas gingivalis lipopolysaccharide (LPS) and its bioactive center, lipid A, are known to exhibit very low endotoxic activities and activate LPS-hyporesponsive C3H/HeJ mice that have a point mutation in the cytoplasmic portion of Toll-like receptor (TLR) 4, in contrast to classical enterobacterial LPS and their lipid A. In the present study, we attempted to determine which TLR mediates the response to lipid A from P. gingivalis strain 381. P. gingivalis LPS and its natural lipid A fraction induced NF-{kappa}B activation primarily in Ba/F3 cells expressing mouse TLR 2 (Ba/mTLR2), rather than in those expressing mouse TLR4 and its accessory protein MD2 (Ba/mTLR4/mMD2). Further purification of the natural lipid A fraction resulted in a significant decrease of NF-{kappa}B activation in Ba/mTLR2, although not in Ba/mTLR4/mMD2. The synthetic counterpart of P. gingivalis strain 381-lipid A (compound PG-381) also elicited NF-{kappa}B activation in Ba/mTLR4/mMD2, but not Ba/mTLR2. Furthermore, P. gingivalis purified natural lipid A and compound PG-381 lacked the ability to activate gingival fibroblasts from C3H/HeJ, TLR4 knockout (KO) and myeloid differentiation factor 88 (MyD88) KO mice. These findings demonstrate that the P. gingivalis lipid A molecule induces cell activation via a TLR4/MD2-MyD88-dependent pathway, and suggest the possibility that unknown bacterial components in P. gingivalis LPS and its lipid A may induce cell activation via TLR2.

Keywords: lipid A, lipopolysaccharide, periodontal disease, Porphyromonas gingivalis, Toll-like receptor


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