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Discrimination of bacterial lipoproteins by Toll-like receptor 6.

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


  • Takeuchi O
  • Kawai T
  • M├╝hlradt PF
  • Morr M
  • Radolf JD
  • Zychlinsky A
  • Takeda K
  • Akira S


International immunology

Publication Data

July 29, 2001

Associated Grants


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