| lipopolysaccharide binding protein binds to triacylated and diacylated lipopeptides and mediates innate immune responses. | lps binding protein (lbp) is an acute-phase protein synthesized predominantly in the liver of the mammalian host. it was first described to bind lps of gram-negative bacteria and transfer it via a cd14-enhanced mechanism to a receptor complex including tlr-4 and md-2, initiating a signal transduction cascade leading to the release of proinflammatory cytokines. in recent studies, we found that lbp also mediates cytokine induction caused by compounds derived from gram-positive bacteria, including ... | 2004 | 15294986 |
| toll-like receptor 2 functions as a pattern recognition receptor for diverse bacterial products. | toll-like receptors (tlrs) 2 and 4 are signal transducers for lipopolysaccharide, the major proinflammatory constituent in the outer membrane of gram-negative bacteria. we observed that membrane lipoproteins/lipopeptides from borrelia burgdorferi, treponema pallidum, and mycoplasma fermentans activated cells heterologously expressing tlr2 but not those expressing tlr1 or tlr4. these tlr2-expressing cells were also stimulated by living motile b. burgdorferi, suggesting that tlr2 recognition of li ... | 1999 | 10559223 |
| activation of human monocytic cells by borrelia burgdorferi and treponema pallidum is facilitated by cd14 and correlates with surface exposure of spirochetal lipoproteins. | here we examined the involvement of cd14 in monocyte activation by motile borrelia burgdorferi and treponema pallidum. b. burgdorferi induced secretion of il-8 by vitamin d3-matured thp-1 cells, which was inhibited by a cd14-specific mab known to block cellular activation by lps and the prototypic spirochetal lipoprotein, outer surface protein a. enhanced responsiveness to b. burgdorferi also was observed when thp-1 cells were transfected with cd14. because borreliae within the mammalian host an ... | 1999 | 10438943 |
| crystal structure at 2.4 a resolution of borrelia burgdorferi inosine 5'-monophosphate dehydrogenase: evidence of a substrate-induced hinged-lid motion by loop 6. | the conversion of inosine 5'-monophosphate (imp) to xanthosine 5'-monophosphate (xmp) is the committed and rate-limiting reaction in de novo guanine nucleotide biosynthesis. inosine 5'- monophosphate dehydrogenase (impdh) is the enzyme that catalyzes the oxidation of imp to xmp with the concomitant reduction of nicotinamide adenine dinucleotide (from nad(+) to nadh). because of its critical role in purine biosynthesis, impdh is a drug design target for anticancer, antiinfective, and immunosuppre ... | 2000 | 10758003 |
| borrelia burgdorferi bind to epithelial cell proteoglycans. | borrelia burgdorferi adhere to mammalian cells in vitro but neither the ligand(s) nor the receptor(s) has (have) been clearly established. using an in vitro attachment-inhibition assay, a b. burgdorferi attachment mechanism has been identified. heparin, heparan sulfate, and dermatan sulfate reduced the attachment of virulent b. burgdorferi strain 297 to hela cells by approximately 60%. in addition, virulent, but not avirulent, b. burgdorferi strains b31, n40, and hb19 demonstrated heparin attach ... | 1994 | 8113413 |