Open AccessIgE epitope analysis of the hevein preprotein; a major latex allergen
Author(s) -
BEEZHOLD D. H.,
KOSTYAL D. A.,
SUSSMAN G. L.
Publication year - 1997
Publication title -
clinical & experimental immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.329
H-Index - 135
eISSN - 1365-2249
pISSN - 0009-9104
DOI - 10.1046/j.1365-2249.1997.d01-983.x
Subject(s) - epitope , latex allergy , immunoglobulin e , allergen , epitope mapping , biology , immunology , chemistry , allergy , antigen , biochemistry , antibody
We have previously identified the hevein preprotein as a common allergen for latex allergic healthcare workers. The B cell epitopes in the hevein protein that are recognized by IgE of latex‐allergic individuals have not been identified. In this study, we examined the hevein preprotein using epitope mapping. Overlapping synthetic peptides of 10 amino acids (two aa overlap) were synthesized on a derivatized cellulose membrane using Fmoc chemistry. The peptide spots were probed with pooled sera from 10 latex‐allergic patients, and the IgE‐reactive peptides identified with anti‐IgE MoAbs. We identified six B cell epitopes within the full length hevein preprotein which bound IgE from latex‐allergic patients. Two were located in the N‐terminal 5‐kD hevein domain and four were observed in the 14‐kD C‐domain. A broad epitope was located between the N‐terminal amino acids 13–24. This epitope had nearly complete homology to wheat germ agglutinin (WGA). Immunological cross‐reactivity to WGA was confirmed by Western blot analysis with purified WGA, and this reactivity could be inhibited by latex proteins or WGA. Of the five remaining epitopes, four had homologies to other proteins in the pathogenesis‐related family of plant proteins (PR‐4). The data demonstrate that hevein has multiple IgE epitopes. The significant homology of these epitopes to a broad family of plant defence proteins further explains the increased prevalence of food allergies in latex‐allergic individuals.