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Lipid modification of the 15 kilo Dalton major membrane immunogen of Treponema pallidum
Author(s) -
Purcell B. K.,
Swancutt M. A.,
Radolf J. D.
Publication year - 1990
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1990.tb00716.x
Subject(s) - immunogen , biology , recombinant dna , treponema , signal peptide , biochemistry , amino acid , signal peptidase , microbiology and biotechnology , peptide , gene , monoclonal antibody , antibody , virology , human immunodeficiency virus (hiv) , immunology , syphilis
Summary The 15 kiloDalton major membrane immunogen was included among the Treponema pallidum polypeptides selectively labelled with [ 3 H]‐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 [ 3 H]‐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.