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Lipid modification of the 15 kilo Dalton major membrane immunogen of Treponema pallidum
Authors:B. K. Purcell  M. A. Swancutt  J. D. Radolf
Affiliation:Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas 75235.
Abstract: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.
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