FATTY-ACIDS OF TREPONEMA-PALLIDUM AND BORRELIA-BURGDORFERI LIPOPROTEINS
FATTY-ACIDS OF TREPONEMA-PALLIDUM AND BORRELIA-BURGDORFERI LIPOPROTEINS
复制标题
DOI：
10.1128/jb.176.8.2151-2157.1994
复制
发表时间：
1994-04-01
影响因子：
3.2
通讯作者：
NORGARD, MV
中科院分区：
文献类型：
--
作者：
BELISLE, JT;BRANDT, ME;NORGARD, MV
螺旋体病原体梅毒螺旋体（Treponema pallidum subsp.）苍白球（T. pallidum）和伯氏疏螺旋体（Borreliaburgdorferi）（分别是性病梅毒和莱姆病的病原体）的区别在于它们最丰富的膜蛋白含有共价连接的脂肪酸。在这项研究中，我们确定了脂肪酸共价结合脂蛋白的B。burgdorferi和T. pallidum和检查这些分子的潜在酰基供体。棕榈酸是两种B的主要脂肪酸。burgdorferi和T.苍白球脂蛋白T.苍白球脂蛋白还含有大量的硬脂酸盐，一种在原核脂蛋白中不常见的脂肪酸。在这两种螺旋体中，细胞脂质的脂肪酸不同于它们各自的脂蛋白。为了表征这些生物体中的磷脂，用[H-3]棕榈酸酯或[H-3]油酸酯代谢标记螺旋体; B。burgdorferi只含有磷脂酰甘油和磷脂酰胆碱，而T.苍白球含有磷脂酰甘油、磷脂酰胆碱、磷脂酰乙醇胺、磷脂酰丝氨酸、磷脂酰肌醇和心磷脂。虽然棕榈酸占主导地位的脂蛋白，有没有明显的差异，这两种脂肪酸纳入磷脂（假定的酰基供体）。磷脂酶A（1）和A（2）消化来自B的磷脂酰胆碱。burgdorferi和T.用[H-3]棕榈酸酯或[H-3]油酸酯标记的苍白球也显示，没有一种脂肪酸优先掺入甘油骨架的1和2位（潜在的酰基供体位点）。综合研究结果表明，脂蛋白合成过程中的脂肪酸利用率在很大程度上取决于脂蛋白酰基转移酶的脂肪酸特异性。这些发现也为阐明脂蛋白酰化与这些分子的生理功能和炎症活性之间的关系提供了基础。
A fundamental ultrastructural feature shared by the spirochetal pathogens Treponema pallidum subsp. pallidum (T. pallidum) and Borrelia burgdorferi, the etiological agents of venereal syphilis and Lyme disease, respectively, is that their most abundant membrane proteins contain covalently attached fatty acids. In this study, we identified the fatty acids covalently bound to lipoproteins of B. burgdorferi and T. pallidum and examined potential acyl donors to these molecules. Palmitate was the predominant fatty acid of both B. burgdorferi and T. pallidum lipoproteins. T. pallidum lipoproteins also contained substantial amounts of stearate, a fatty acid not typically prevalent in prokaryotic lipoproteins. In both spirochetes, the fatty acids of cellular lipids differed from those of their respective lipoproteins. To characterize phospholipids in these organisms, spirochetes were metabolically labeled with [H-3]palmitate or [H-3]oleate; B. burgdorferi contained only phosphatidylglycerol and phosphatidylcholine, while T. pallidum contained phosphatidylglycerol, phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, phosphatidylinositol, and cardiolipin. Although palmitate predominated in the lipoproteins, there were no apparent differences in the incorporation of these two fatty acids into phospholipids (putative acyl donors). Phospholipase A(1) and A(2) digestion of phosphatidylcholine from B. burgdorferi and T. pallidum labeled with either [H-3]palmitate or [H-3]oleate also revealed that neither fatty acid was incorporated preferentially into the 1 and 2 positions (potential acyl donor sites) of the glycerol backbone. The combined findings suggest that fatty acid utilization during lipoprotein synthesis is determined largely by the fatty acid specificities of the lipoprotein acyl transferases. These findings also provide the basis for ongoing efforts to elucidate the relationship between lipoprotein acylation and the physiological functions and inflammatory activities of these molecules.