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Cutting Edge |
* Department of Host Defense, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan;
Solution Oriented Research for Science and Technology, Japan Science and Technology Corporation, Osaka, Japan;
Department of Cancer Biology, University of Texas M. D. Anderson Cancer Center, Houston, TX 77030; and
Division of Dermatology, Department of Microbiology and Immunology and Molecular Biology Institute, University of California, Los Angeles, School of Medicine, Los Angeles, CA 90095
The Toll-like receptor (TLR) family acts as pattern recognition
receptors for pathogen-specific molecular patterns (PAMPs). TLR2 is
essential for the signaling of a variety of PAMPs, including bacterial
lipoprotein/lipopeptides, peptidoglycan, and GPI anchors. TLR6
associates with TLR2 and recognizes diacylated mycoplasmal lipopeptide
along with TLR2. We report here that TLR1 associates with TLR2 and
recognizes the native mycobacterial 19-kDa lipoprotein along with TLR2.
Macrophages from TLR1-deficient (TLR1-/-) mice showed
impaired proinflammatory cytokine production in response to the 19-kDa
lipoprotein and a synthetic triacylated lipopeptide. In contrast,
TLR1-/- cells responded normally to diacylated
lipopeptide. TLR1 interacts with TLR2 and coexpression of TLR1 and TLR2
enhanced the NF-
B activation in response to a synthetic lipopeptide.
Furthermore, lipoprotein analogs whose acylation was modified were
preferentially recognized
by
TLR1. Taken together, TLR1 interacts with TLR2 to recognize the lipid
configuration of the native mycobacterial lipoprotein as well as
several triacylated lipopeptides.
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