Lipid modification of the 15 kiloDalton major membrane immunogen of Treponema pallidum

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acylation
  • Amino Acid Sequence
  • Antigens, Bacterial / genetics
  • Antigens, Bacterial / immunology
  • Antigens, Bacterial / metabolism*
  • Base Sequence
  • Cell-Free System
  • Cloning, Molecular
  • Consensus Sequence
  • Genes, Bacterial
  • Immunoblotting
  • Lipid Metabolism*
  • Molecular Sequence Data
  • Restriction Mapping
  • Transformation, Genetic
  • Treponema pallidum / genetics
  • Treponema pallidum / immunology*
  • Treponema pallidum / metabolism


  • Antigens, Bacterial
  • major membrane immunogen, Treponema pallidum 15K

Associated data

  • GENBANK/M30941