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. 1996 Jan 16;189(1):137-40.
doi: 10.1016/0022-1759(95)00254-5.

Detection of antigenic determinants in the Treponema pallidum membrane protein TmpA using overlapping synthetic peptides

G Antoni  1 , G dal Maso, B Berti, C Soldatini, F Cocola
Affiliations

Detection of antigenic determinants in the Treponema pallidum membrane protein TmpA using overlapping synthetic peptides

G Antoni et al. J Immunol Methods. .

Abstract

The antigenic structure of the 42 kDa membrane protein of Treponema Pallidum, TmpA, was studied using synthetic peptides. Ten overlapping peptides, 35-40 residues each, were synthesized in order to cover the entire sequence of the molecule. The antigenic activity of the fragments was examined by enzyme-linked immunosorbent assay (ELISA). In this way it was possible to demonstrate a significant antigenic activity of four peptides which were reactive with syphilitic sera. The N-terminal fragment TmpA1, 38 residues long, proved to be the most reactive. Its antigenic structure was therefore studied in more detail, by examining shorter fragments. The N-terminal portion of TmpA1, consisting of 19 residues, (ASGAKEEAEKKAAEQRALL) represents an important fragment of the molecule, and was specifically interactive with most of the syphilitic sera examined.

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