tailieunhanh - Báo cáo khoa học: Physicochemical characterization and biological activity of a glycoglycerolipid from Mycoplasma fermentans

We report a comprehensive physicochemical characteriza-tion of a glycoglycerolipid from Mycoplasma fermentans, MfGl-II, in relation to its bioactivityand compared thiswith the respective behaviors of phosphatidylcholine (PC) and a bacterial glycolipid, lipopolysaccharide (LPS) from deep rough mutantSalmonella minnesotastrain R595. Theb«a gel-to-liquid crystalline phase transition behavior of the hydrocarbon chains withTc¼30 Cfor MfGl-II as well as for LPS exhibits high similarity between the two glycolipids. A lipopolysaccharide-binding protein (LBP)-mediated incorporation into negatively charged liposomes is observed for both glycolipids. . | Eur. J. Biochem. 270 3271-3279 2003 FEBS 2003 doi Physicochemical characterization and biological activity of a glycoglycerolipid from Mycoplasma fermentans Klaus Brandenburg1 Frauke Wagner1 Mareike Muller1 Holger Heine1 Jorg Andra1 Michel H. J. Koch2 Ulrich Zahringer1 and Ulrich Seydel1 1 Forschungszentrum Borstel Center for Medicine and Biosciences Borstel 2European Molecular Biology Laboratory Outstation Hamburg Hamburg Germany We report a comprehensive physicochemical characterization of a glycoglycerolipid from Mycoplasma fermentans MfGl-II in relation to its bioactivity and compared this with the respective behaviors of phosphatidylcholine PC and a bacterial glycolipid lipopolysaccharide LPS from deep rough mutant Salmonella minnesota strain R595. The b a gel-to-liquid crystalline phase transition behavior of the hydrocarbon chains with Tc 30 C for M Gll-H as well as for LPS exhibits high similarity between the two glycolipids. A lipopolysaccharide-binding protein LBP -mediated incorporation into negatively charged liposomes is observed for both glycolipids. The determination of the supramole-cular aggregate structure confirms the existence of a mixed unilamellar cubic structure for MfGl-II similar to that observed for the lipid A moiety of LPS. The biological data clearly show that MfGl-II is able to induce cytokines such as tumor necrosis factor-a TNF-a in human mononuclear cells although to a significantly lower degree than LPS. In contrast in the Limulus amebocyte lysate test MfGl-II is completely inactive and in the CHO reporter cell line it does not indicate any reactivity with the Toll-like receptors TLR-2 and -4 in contrast to control lipopeptides and LPS. These data confirm the applicability of our conformational concept of endotoxicity to nonlipid A structures an amphiphilic molecule with a nonlamellar cubic aggregate structure corresponding to a conical conformation of the single molecules and a sufficiently high .

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