Physicochemical characterization and biological activity of a glycoglycerolipid from Mycoplasma fermentans
Physicochemical characterization and biological activity of a glycoglycerolipid from Mycoplasma fermentans
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DOI:
10.1046/j.1432-1033.2003.03719.x
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发表时间:
2003-08-01
期刊:
影响因子:
--
通讯作者:
Seydel, U
中科院分区:
文献类型:
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作者:
Brandenburg, K;Wagner, F;Seydel, U
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 betaalpha gel-to-liquid crystalline phase transition behavior of the hydrocarbon chains with T (c) = 30 degreesC for 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. The determination of the supramolecular 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-alpha (TNF-alpha) 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 negative charge density in the backbone.