Purcell B K, Swancutt M A, Radolf J D
Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas 75235.
Mol Microbiol. 1990 Aug;4(8):1371-9. doi: 10.1111/j.1365-2958.1990.tb00716.x.
The 15 kiloDalton major membrane immunogen was included among the Treponema pallidum polypeptides selectively labelled with [3H]-palmitate. The cloned gene for this immunogen, tpp15, encoded a signal peptide of 17 amino acids, a consensus signal peptidase II cleavage site, and a mature protein of 124 amino acids (13,967 Daltons). As predicted by the DNA sequence, the recombinant 15 kiloDalton immunogen labelled selectively with [3H]-palmitate, and globomycin inhibited processing of the precursor to the mature polypeptide. While the native and recombinant immunogens are amphiphilic, the 15 kiloDalton immunogen synthesized in a cell-free system was hydrophilic. The covalent attachment of fatty acids appears to be responsible for the amphiphilicity of the immunogen and its membrane attachment.
15千道尔顿主要膜免疫原包含在梅毒螺旋体经[3H] - 棕榈酸选择性标记的多肽中。该免疫原的克隆基因tpp15编码一个17个氨基酸的信号肽、一个共有信号肽酶II切割位点以及一个124个氨基酸（13,967道尔顿）的成熟蛋白。正如DNA序列所预测的，重组15千道尔顿免疫原经[3H] - 棕榈酸选择性标记，并且球霉素抑制前体向成熟多肽的加工。虽然天然和重组免疫原都是两亲性的，但在无细胞系统中合成的15千道尔顿免疫原是亲水性的。脂肪酸的共价连接似乎是免疫原两亲性及其与膜附着的原因。
