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Host Recognition of Bacterial Muramyl Dipeptide Mediated through NOD2
NOD2 mediates the host response to bacterial muropeptides derived from peptidoglycan, an activity that is important for protection against Crohn's disease and has implications for understanding adjuvant function and effective vaccine development.
An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid
It is reported that NOD1 mediates selective recognition of bacteria through detection of iE-DAP-containing peptidoglycan derived primarily from Gram-negative bacteria.
Virulence factors of Yersinia pestis are overcome by a strong lipopolysaccharide response
It is shown that the ability to evade the LPS-induced inflammatory response is critical for Y. pestis virulence, and evasion of TLR4 activation by lipid A alteration may contribute to the virulence of various Gram-negative bacteria.
Toll-like receptor 4 imparts ligand-specific recognition of bacterial lipopolysaccharide.
Data suggest that TLR4 is the central lipid A-recognition protein in the LPS receptor complex, which is likely to be responsible for the species-specific pharmacology of LPS.
Monomeric and polymeric gram-negative peptidoglycan but not purified LPS stimulate the Drosophila IMD pathway.
Lipid A antagonist, lipid IVa, is distinct from lipid A in interaction with Toll-like receptor 4 (TLR4)-MD-2 and ligand-induced TLR4 oligomerization.
L ligand-induced TLR4 oligomerization, homotypic interaction ofTLR4, which directly leads to TLR3 signaling, and MD-2 has an important role in a link between ligand interaction and TLR 4 oligomerized.
Human MD-2 confers on mouse Toll-like receptor 4 species-specific lipopolysaccharide recognition.
The chimeric complex consisting of mTLR4 and hMD-2 was examined to ask whether species specificity is conferred by TLR4 or MD-2, and it was found that hMD -2 was clearly distinct from mMD-1 in the way of influencing LPS recognition by mTLr4.
Lipopolysaccharide Interaction with Cell Surface Toll-like Receptor 4-MD-2
Direct LPS interaction with cell surface TLR4-MD-2 that is distinct from that with MD-2 or CD14 is revealed, suggesting a role for CD14 in LPS loading onto TLR2 but not in the interaction itself between LPS and TLR3-MD2.
Human Peptidoglycan Recognition Protein-L Is an N-Acetylmuramoyl-L-alanine Amidase*
It is reported that human PGRP-L is a Zn2+-dependent N-acetylmuramoyl-l-alanine amidase, an enzyme that hydrolyzes the amide bond between MurNAc and l-Ala of bacterial PGN and this function is conserved in prokaryotes, insects, and mammals.
Bacterial endotoxin: Chemical constitution, biological recognition, host response, and immunological detoxification.
Endotoxins, due to their various potent biological activities soon attracted worldwide scientific interest, were first found to be produced by Vibrio cholerae bacteria and later by Salmonella and Serratia.