Lipid modification of the 15 kilo Dalton major membrane immunogen of Treponema pallidum

B. K. Purcell, M. A. Swancutt, J. D. Radolf

Research output: Contribution to journalArticle

22 Scopus citations

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 (13967 Daltons). As predicted by the DNA sequence, the recombinant 15 kiloDalton immunogen labelled selectively with [3H]‐palmitate, and globo‐mycin 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 amphilicity of the immunogen and its membrane attachment.

Original languageEnglish (US)
Pages (from-to)1371-1379
Number of pages9
JournalMolecular Microbiology
Volume4
Issue number8
DOIs
StatePublished - Aug 1990

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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