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Discrimination of bacterial lipoproteins by Toll-like receptor 6.

International immunology | Jul 29, 2001

http://www.ncbi.nlm.nih.gov/pubmed/11431423

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.

Pubmed ID: 11431423 RIS Download

Mesh terms: Animals | Bacterial Proteins | Cells, Cultured | Drosophila Proteins | Humans | Interleukin-12 | Interleukin-6 | Lipopeptides | Lipoproteins | Macrophages, Peritoneal | Membrane Glycoproteins | Mice | Mice, Inbred A | Mice, Inbred C57BL | Mice, Knockout | NF-kappa B | Nitric Oxide | Oligopeptides | Receptors, Cell Surface | Signal Transduction | Toll-Like Receptor 2 | Toll-Like Receptor 6 | Toll-Like Receptors | Tumor Necrosis Factor-alpha

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Mouse Genome Informatics (Data, Gene Annotation)

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