
Mapping of B cell epitopes in an immunodominant antigen of Trypanosoma cruzi using fusions to the Escherichia coli LamB protein
Author(s) -
Pereira Cátia M,
Yamauchi Lucy M,
Levin Mariano J,
Silveira José Franco,
Castilho Beatriz A
Publication year - 1998
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1998.tb13077.x
Subject(s) - immunogen , epitope , biology , antigen , immunodominance , fusion protein , microbiology and biotechnology , antibody , linear epitope , escherichia coli , virology , epitope mapping , peptide sequence , tandem repeat , trypanosoma cruzi , recombinant dna , monoclonal antibody , biochemistry , genetics , gene , parasite hosting , world wide web , computer science , genome
The JL8 protein antigen from Trypanosoma cruzi , a dominant immunogen in man, has been characterized as containing tandem amino acid repeats. Here, we describe the use of the LamB protein of Escherichia coli as a carrier of JL8 derived sequences in order to map the immunodominant B cell epitopes in this antigen. Five different sequences of JL8 were inserted in the LamB protein and the JL8‐LamB fusion proteins were tested by ELISA with human chronic chagasic sera. The fusion carrying the sequence AEKQKAAEATKVAE was recognized by most sera. This protein was also capable of inhibiting the binding of human chagasic antibodies to GST‐JL8 in competitive ELISA suggesting that it contains an immunodominant B cell epitope of JL8.