Mapping of antigenic determinants of the T. cruzi hsp70 in chagasic and healthy individuals

• Published in: Molecular immunology Vol. 30; no. 12; p. 1115
• Main Authors: Requena, J M, Soto, M, Guzman, F, Maekelt, A, Noya, O, Patarroyo, M E, Alonso, C
• Format: Journal Article
• Language: English
• Published: England 01.08.1993
• Subjects: Amino Acid Sequence; Animals; Chagas Disease - immunology; Heat-Shock Proteins - immunology; Humans; Molecular Sequence Data; Peptides - chemistry; Peptides - immunology; Sequence Alignment; Trypanosoma cruzi - immunology
• ISSN: 0161-5890
• DOI: 10.1016/0161-5890(93)90158-8

In the present paper we describe the analysis of the immunological recognition by sera of healthy individuals and chagasic patients of the Trypanosoma cruzi heat shock 70 kDa protein. By a Falcon Assay Screening Test, using as antigen an ATP-agarose purified T. cruzi hsp70, it has been found that the sera of infected patients as well as of that of healthy individuals show reactivity against the hsp70 protein but that the reactivity of the sera of patients is in general significantly higher than that of healthy individuals. The analysis of the reactivity of the chagasic sera against a collection of peptides covering 92% of the protein has shown that more than 50% of the peptides gave a positive response but only against a few peptides did we observe high reactivity in a wide spectrum of sera. Only four peptides (numbers 9, 12, 14 and 47) were recognized by all sera tested with high reactivity values. The sera of healthy individuals also showed reactivity against a large percentage of peptides but with lower values. It was observed that particular peptides showing high reactivity against the sera of healthy donors also show high reactivity against patients' sera. However, the general pattern of reactivity against the peptides is different in chagasic and healthy sera. The immunodominant peptides map in the highly conserved as well as in the less conserved part of the hsp70 molecule. The 1/3 C-terminal, being the least conserved part of the molecule, seems to be the least immunogenic. Mapping of the epitopes led to the identification of particular immunogenic motifs within individual peptides.