TY - JOUR
T1 - Lipid modification of the 15 kilo Dalton major membrane immunogen of Treponema pallidum
AU - Purcell, B. K.
AU - Swancutt, M. A.
AU - Radolf, J. D.
PY - 1990/8
Y1 - 1990/8
N2 - 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.
AB - 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.
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U2 - 10.1111/j.1365-2958.1990.tb00716.x
DO - 10.1111/j.1365-2958.1990.tb00716.x
M3 - Article
C2 - 2280688
AN - SCOPUS:0025178972
SN - 0950-382X
VL - 4
SP - 1371
EP - 1379
JO - Molecular Microbiology
JF - Molecular Microbiology
IS - 8
ER -