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 and Bruce Beutler ()
Additional contact information
Kasper Hoebe: The Scripps Research Institute
Philippe Georgel: The Scripps Research Institute
Sophie Rutschmann: The Scripps Research Institute
Xin Du: The Scripps Research Institute
Suzanne Mudd: The Scripps Research Institute
Karine Crozat: The Scripps Research Institute
Sosathya Sovath: The Scripps Research Institute
Louis Shamel: The Scripps Research Institute
Thomas Hartung: EU Joint Research Centre, ECVAM
Ulrich Zähringer: Leibniz-Center for Medicine and Biosciences
Bruce Beutler: The Scripps Research Institute

Nature, 2005, vol. 433, issue 7025, 523-527

Abstract: Abstract 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.

Date: 2005
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DOI: 10.1038/nature03253

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