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Epitope Specificity of a Monoclonal Antibody Generated against the Dissociated CFA/I Fimbriae of Enterotoxigenic Escherichia coli
Author(s) -
De Luna Maria Das Graças,
Rudin Anna,
Vinhas Solange Alves,
Almeida Darcy Fontoura,
Souza Ferreira Luis Carlos
Publication year - 1998
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.1998.tb02293.x
Subject(s) - enterotoxigenic escherichia coli , fimbria , epitope , monoclonal antibody , biology , microbiology and biotechnology , pilus , hemagglutination , bacterial adhesin , escherichia coli , flagellin , fimbriae proteins , polyclonal antibodies , enterobacteriaceae , antigen , antibody , biochemistry , enterotoxin , receptor , immunology , gene , genetics
A monoclonal antibody (MAb 84) raised against the dissociated CFA/I fimbriae of enterotoxigenic Escherichia coli was characterized with regard to antigen binding and epitope specificity. Enzyme‐linked immunosorbent assay (ELISA) showed that MAb 84 had higher affinity to CFA/I subunits than to intact CFA/I fimbriae and recognized a Salmonella flagellin carrying an insert corresponding to amino acids 32 to 45 of the CFA/I subunit. Fine epitope mapping based on the Pepscan technique showed that the peptide 39 TFESY 43 , derived from the sequence of the mature CFA/I subunit, was specifically recognized by MAb 84. The 39 TFESY 43 sequence is probably not accessible on the surface of the native CFA/I fimbriae since MAb 84 did not bind to intact fimbriae as evaluated in inhibition ELISA tests. Moreover, MAb 84 did not agglutinate fimbriated ETEC cells nor inhibit CFA/I‐mediated hemagglutination or the adhesion to Caco‐2 cells.