Acylation and immunological properties of Mycoplasma gallisepticum membrane proteins
Acylation and immunological properties of Mycoplasma gallisepticum membrane proteins
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DOI：
10.1016/0923-2508(96)81070-9
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发表时间：
1995-11-01
影响因子：
2.6
通讯作者：
Wroblewski, H
中科院分区：
文献类型：
--
作者：
Jan, G;Fontenelle, C;Wroblewski, H
用不同的C-14-脂肪酸标记鸡毒支原体膜蛋白，用电泳法和化学分析法研究其酰化反应，并用免疫印迹和交叉免疫电泳法研究其免疫学性质。在双向电泳法分离的200多个膜多肽中，有35个组分(包括主要蛋白p67)被酰基链共价修饰。这些酰化蛋白的pL值低于平均值(5.0~7.4vs.5.0~9.0)，是鸡毒支原体的主要膜蛋白抗原和免疫原。体内标记结果表明，脂肪酸与蛋白质结合的表观选择性为：棕榈酸(16：0)>；肉豆蔻酸(14：0)>；油酸(18：1C)>；硬脂酸(18：0)>；亚油酸(18：2C)。化学分析表明，其选择性顺序为18：2C>；16：0>；18：1C>；18：0>；14：0，即棕榈酸是主要的O-酯结合脂肪酸，亚油酸是主要的酰胺键脂肪酸。观察到的[O-酯结合+酰胺连接的酰链]/O-酯结合链的平均比值接近1.4，以及S甘油半胱氨酸的存在表明，在鸡败血杆菌中，膜蛋白的脂质修饰机制与革兰氏阴性真细菌的脂蛋白相同。
The acylation of Mycoplasma gallisepticum membrane proteins was studied by electrophoresis after in vivo labelling with different C-14-fatty acids and by chemical analysis, The immunological properties of these proteins were investigated by Western blotting and crossed immunoelectrophoresis. Among the ca, 200 membrane polypeptides resolved by two-dimensional electrophoresis, 35 components (including the major protein p67) were covalently modified with acyl chains. These acylated proteins displayed lower pls than average (5.0-7.4 vs. 5.0-9.0) and proved to be the major membrane protein antigens and immunogens of M. gallisepticum. The apparent selectivity of fatty acid incorporation into proteins was, as suggested by in vivo labelling: palmitic acid (16:0)>myristic acid (14:0)>oleic acid (18:1c)>stearic acid (18:0)>linoleic acid (18:2c). However, the true order of selectivity, as revealed by chemical analysis, proved to be 18:2c> 16:0> 18:1c> 18:0> 14:0, More specifically, palmitic acid was the major O-ester-bound fatty acid and linoleic acid the major amide-linked fatty acid. The observed average ratio [O-ester-bound+amide-linked acyl chains]/O-ester-bound chains approximate to 1.4 and the presence of S-glycerylcysteine suggest that, in M, gallisepticum, membrane proteins are lipid-modified according to a mechanism identical to that depicted for lipoproteins of Gram-negative eubacteria.