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TY - JOUR AU - Hoebe, Kasper AU - Georgel, Philippe AU - Rutschmann, Sophie AU - Du, Xin AU - Mudd, Suzanne AU - Crozat, Karine AU - Sovath, Sosathya AU - Shamel, Louis AU - Hartung, Thomas AU - Zähringer, Ulrich AU - Beutler, Bruce PY - 2005 DA - 2005/02/01 TI - CD36 is a sensor of diacylglycerides JO - Nature SP - 523 EP - 527 VL - 433 IS - 7025 AB - Toll-like receptor 2 (TLR2) is required for the recognition of numerous molecular components of bacteria1,2,3,4,5,6,7,8, fungi9,10 and protozoa11. The breadth of the ligand repertoire seems unusual, even if one considers that TLR2 may form heteromers with TLRs 1 and 6 (ref. 12), and it is likely that additional proteins serve as adapters for TLR2 activation. Here we show that an N-ethyl-N-nitrosourea-induced nonsense mutation of Cd36 (oblivious) causes a recessive immunodeficiency phenotype in which macrophages are insensitive to the R-enantiomer of MALP-2 (a diacylated bacterial lipopeptide) and to lipoteichoic acid. Homozygous mice are hypersusceptible to Staphylococcus aureus infection. Cd36obl macrophages readily detect S-MALP-2, PAM2CSK4, PAM3CSK4 and zymosan, revealing that some—but not all—TLR2 ligands are dependent on CD36. Already known as a receptor for endogenous molecules, CD36 is also a selective and nonredundant sensor of microbial diacylglycerides that signal via the TLR2/6 heterodimer. SN - 1476-4687 UR - https://doi.org/10.1038/nature03253 DO - 10.1038/nature03253 ID - Hoebe2005 ER -