CD36 is a sensor of diacylglycerides

Kasper Hoebe, Philippe Georgel, Sophie Rutschmann, Xin Du, Suzanne Mudd, Karine Crozat, Sosathya Sovath, Louis Shamel, Thomas Hartung, Ulrich Zähringer, Bruce Beutler

Research output: Contribution to journalArticlepeer-review

700 Scopus citations


Toll-like receptor 2 (TLR2) is required for the recognition of numerous molecular components of bacteria, fungi and protozoa. 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, PAM 3CSK4 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.

Original languageEnglish (US)
Pages (from-to)523-527
Number of pages5
Issue number7025
StatePublished - Feb 3 2005

ASJC Scopus subject areas

  • General


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