摘要
CD14 has been shown to enhance Toll-like receptor 2 (TLR2)-mediated signaling in response to peptidoglycan. Anti-CD14 monoclonal antibody MEM-18, whose epitope was located at the amino acid residues 57芒芒芒64, blocked the binding of sCD14 to the recombinant soluble form of the extracellular TLR2 domain (sTLR2). The deletion mutant sCD14芒芒57芒芒芒64 lacking the amino acid residues 57芒芒芒64 failed to bind to sTLR2. Cotransfection of wild type mCD14 but not mCD14芒芒57芒芒芒64 with TLR2 enhanced NF-芒芒B activation in response to peptidoglycan. These results indicate that the CD14 region spanning amino acids 57芒芒芒64 is critical for interacting with TLR2 and enhancing TLR2-mediated peptidoglycan signaling.