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International Immunology, Vol. 13, No. 7, 933-940, July 2001
© 2001 Japanese Society for Immunology

Discrimination of bacterial lipoproteins by Toll-like receptor 6

Osamu Takeuchi1,2, Taro Kawai1,2, Peter F. Mühlradt3, Michael Morr3, Justin D. Radolf4, Arturo Zychlinsky5, Kiyoshi Takeda1,2 and Shizuo Akira1,2 1 Department of Host Defense, Research Institute for Microbial Diseases, Osaka University, and
2 Core Research for Evolutional Science and Technology (CREST) of Japan Science and Technology Corp., 3-1 Yamada-oka, Suita, Osaka 565-0871, Japan
3 Immunobiology Research Group, Gesellschaft für Biotechnologische Forschung, Mascheroderweg 1, 38124 Braunschweig, Germany
4 Center for Microbial Pathogenesis, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, CT 06030, USA
5 Skirball Institute and Department of Microbiology, New York University School of Medicine, 540 First Avenue, New York, NY 10016, USA

Correspondence to: S. Akira

Bacterial lipoproteins (BLP) trigger immune responses via Toll-like receptor 2 (TLR2) and their immunostimulatory properties are attributed to the presence of a lipoylated N-terminus. Most BLP are triacylated at the N-terminus cysteine residue, but mycoplasmal macrophage-activating lipopeptide-2 kD (MALP-2) is only diacylated. Here we show that TLR6-deficient (TLR6–/–) cells are unresponsive to MALP-2 but retain their normal responses to lipopeptides of other bacterial origins. Reconstitution experiments in TLR2–/– TLR6–/– embryonic fibroblasts reveal that co-expression of TLR2 and TLR6 is absolutely required for MALP-2 responsiveness. Taken together, these results show that TLR6 recognizes MALP-2 cooperatively with TLR2, and appears to discriminate between the N-terminal lipoylated structures of MALP-2 and lipopeptides derived from other bacteria.

Keywords: cytokine, inflammatory mediator, knockout, macrophage, monocyte, transgenic

Transmitting editor: T. Watanabe


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