Discrimination of bacterial lipoproteins by Toll-like receptor 6

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ID: 295743
2001
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Abstract
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.
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Authors Osamu Takeuchi, Taro Kawai, Peter F. Mühlradt, Michael Morr, Justin D. Radolf, Arturo Zychlinsky, Kiyoshi Takeda, Shizuo Akira
Journal international immunology
Year 2001
DOI
10.1093/intimm/13.7.933
URL
https://academic.oup.com/intimm/article-pdf/13/7/933/18321205/130933.pdf
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