CD36 is a sensor of diacylglycerides
Abstract
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. Cd36(obl) macrophages readily detect S-MALP-2, PAM(2)CSK(4), PAM(3)CSK(4) 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.
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CD36 mediates heterodimer formation of TLR4 and TLR6.
“CD36 mediates heterodimer formation of TLR4 and TLR6 (REF. 104), and this co-receptor complex upregulates the production of chemokines and cytokines such as pro-IL-1β through the activation of NF-κb.”
From Sterile inflammation: sensing and reacting to damage (2010) · cites this paper as [104]
The CD36/TLR4/TLR6 co-receptor complex upregulates production of chemokines and cytokines such as pro-IL-1β through activation of NF-κB.
“CD36 mediates heterodimer formation of TLR4 and TLR6 (REF. 104), and this co-receptor complex upregulates the production of chemokines and cytokines such as pro-IL-1β through the activation of NF-κb.”
From Sterile inflammation: sensing and reacting to damage (2010) · cites this paper as [104]
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References 25 · Cited by 873
- Authors
- Hoebe, K., Georgel, P., Rutschmann, S., Du, X., Mudd, S., Crozat, K., Sovath, S., Shamel, L., Hartung, T., Zähringer, U., & Beutler, B.
- Affiliations
- Scripps Research Institute (US)
- Research Center Borstel - Leibniz Lung Center (DE)
- Corresponding author
- Beutler, Bruce
- Venue
- Nature
- Published
- 2005-02
- Volume
- 433
- Issue
- 7025
- Pages
- 523-527
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2069663822
- Cited by
- 873
- References
- 25
- Citations by year
- 2026: 11 · 2025: 12 · 2024: 18 · 2023: 13 · 2022: 14 · 2021: 24 · 2020: 23 · 2019: 19 · 2018: 25 · 2017: 29 · 2016: 39 · 2015: 38 · 2014: 47 · 2013: 56 · 2012: 47
- FWCI
- 31.19
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
- Keywords
- CD36, diacylglycerol, TLR2, MALP-2, lipoteichoic acid, Staphylococcus aureus infection, zymosan, bacterial lipopeptides, innate immunity, nonsense mutation
- MeSH terms
- Aging, Animals, Cell Line, Ethylnitrosourea, Glycerides, Homozygote, Humans, Immunologic Deficiency Syndromes, Membrane Glycoproteins, Mice, Inbred C57BL, Mutation, Oligopeptides, Peptidoglycan, Phenotype, Receptors, Cell Surface, Staphylococcal Infections, Staphylococcus aureus, Tumor Necrosis Factor-alpha, Zymosan, Signal Transduction, Mutagenesis, Gene Deletion, Mice, Knockout, CD36 Antigens, Dimerization, Toll-Like Receptors, Toll-Like Receptor 2, Mice, Lipopeptides
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