IgE-Mediated Allergic Reactions to Potatoes

Wahl, R.; Lau, Susanne; Maasch, H.J.; Wahn, Ulrich

doi:10.1159/000235209

Cited by 23 publications

(8 citation statements)

References 15 publications

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“…Of the six epitopes identified, four were common to proteins in this family. The homology of hevein epitopes to the wound-inducible proteins of potato (WIN1, WIN2) as well as previously observed homology of a 46-kD latex protein to the potato storage protein patatin [23] explain the finding that 40% of latexallergic patients had skin test reactivity to potato, an otherwise rare allergen [28,29]. The existence of multiple epitopes for IgE in conserved regions of common plant defence proteins provides the mechanism for multiple cross-reactivities.…”

Section: Discussionmentioning

confidence: 75%

IgE epitope analysis of the hevein preprotein; a major latex allergen

Beezhold

Kostyal

Sussman

1997

Clinical and Experimental Immunology

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SUMMARYWe 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 latexallergic 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.

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Section: Discussionmentioning

confidence: 75%

IgE epitope analysis of the hevein preprotein; a major latex allergen

Beezhold

Kostyal

Sussman

1997

Clinical and Experimental Immunology

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“…Sensitization to potato is documented, and IgE binding is demonstrated for several potato proteins using Western blotting (8). Sensitization to potato often occurs in combination with birch pollen allergy (9)(10)(11).…”

Section: Introductionmentioning

confidence: 99%

Effect of Heat-Induced Aggregation on the IgE Binding of Patatin (Sol t 1) Is Dominated by Other Potato Proteins

Koppelman

Koningsveld

Knulst

et al. 2002

J. Agric. Food Chem.

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The interaction of the major potato allergen patatin, Sol t 1, with IgE was investigated on a quantitative level as a function of heat treatment at different temperatures. On the basis of a number of publications, potato is considered to be a heat-labile allergen, but the molecular explanation for this behavior was not given. In this work, heat treatment of patatin in the absence and presence of other potato proteins mimicking the proteinaceous environment of the potato was studied. Using far-UV circular dichrosim spectroscopy, tryptophan fluorescence spectroscopy, and differential scanning calorimetry, the molecular transitions during heating of patatin were investigated. It was found that as long as patatin is not aggregated, denaturation of patatin on a secondary or tertiairy folding level is reversible with only a minor effect on the IgE affinity. Aggregation of patatin results in a nonreversible unfolding and a concomitant important decrease in affinity for IgE (25-fold). Aggregation of patatin in the presence of other potato proteins results in a less condensed aggregate compared to the situation of isolated patatin, resulting in a more pronounced decrease of affinity for IgE (110-fold). It is concluded that the heat lability of patatin-IgE interaction is explained by aggregation of patatin with other potato proteins rather than by denaturation of patatin itself.

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“…In our study of the Korean population, only one allergenic protein (45 kDa) could be identified as the major allergen, and it was present in extracts from wild-type and GM potatoes. Moreover, this protein may be the same one identified in a previous investigation [23]. Proteolytic stability is a useful criterion in assessing the allergenic potential of food allergens.…”

Section: Discussionmentioning

confidence: 79%