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Immunoblotting in the diagnosis of cross-reactivity in children allergic to birch.
Rocz Akad Med Bialymst. 2005; 50:268-73.RA

Abstract

PURPOSE

The scientific experiments with new immunological methods (immunoblotting, RAST inhibition) and isolation of recombinant allergens suggest structural similarities in the allergenic components responsible for cross-reactions. Immunochemical and molecular biology studies indicate that epitopes of major allergen (Bet v 1, Mal d 1) contain more IgE binding epitopes than minor allergens (Bet v 2, Mal d 2), what explained clinical importance of major birch and apple allergens, but it is individual. The important role in cross-reactivity play also proteins with low molecular weight; a potentially dangerous allergen is lipid transfer protein (LTP) inducing severe systemic reactions in allergic subjects. The recent studies indicate that the IgE cross-reactivity patterns and the clinical relevance is still not clear and that only some of patients with confirmed IgE cross allergy to Bet v 1 and Mal d 1 demonstrated clinical symptoms after ingesting of apple. The aim of study was to establish the pattern of cross-reactivity between major (Bet v 1) and minor (Bet v 2) birch pollen allergens and apple proteins in children allergic to birch using recombinant allergens and immunoblotting method.

MATERIAL AND METHODS

The prospective study were carried out on the group of 13 children aged 4-16 years, referred to the IIIrd Department of Paediatrics in Białystok and outpatient clinic with clinical symptoms of food and inhalant allergy. Inclusion criteria to the study were: allergy to birch pollen recombinant allergens and apple, confirmed by presence of specific IgE in the sera of patients. The allergens from peel and pulp of apple and birch were separated and loaded onto the polyacrylamide electrophoretic gel and than transferred to membranes by Western blotting. Antigen-IgE complex was detected using goat anti-human IgE antibodies labelled with alkaline phosphatase.

RESULTS

Only few sera presented strong reactions in immunoblotting to birch pollen proteins with a molecular weight of 17-18 kDa, corresponding to the main birch allergen Bet v 1. Most of sera having positive reaction vs Bet v 1 showed cross-reactivity with Mal d 1. All sera recognized specifically the main allergen of apple peel Mal d 3 with molecular weight < 10 kDa (Lipid Transfer Protein).

CONCLUSIONS

Immunoblotting method allows to verification of cross-reactivity recognized by presence of specific IgE. The nature of proteins responsible for sensitization can influence the spectrum of offending foods and the clinical features of allergic reactions.

Authors+Show Affiliations

III Department of Paediatrics, Medical University of Białystok, Poland. becud@wp.plNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16358981

Citation

Cudowska, B, et al. "Immunoblotting in the Diagnosis of Cross-reactivity in Children Allergic to Birch." Roczniki Akademii Medycznej W Bialymstoku (1995), vol. 50, 2005, pp. 268-73.
Cudowska B, Kaczmarski M, Restani P. Immunoblotting in the diagnosis of cross-reactivity in children allergic to birch. Rocz Akad Med Bialymst. 2005;50:268-73.
Cudowska, B., Kaczmarski, M., & Restani, P. (2005). Immunoblotting in the diagnosis of cross-reactivity in children allergic to birch. Roczniki Akademii Medycznej W Bialymstoku (1995), 50, 268-73.
Cudowska B, Kaczmarski M, Restani P. Immunoblotting in the Diagnosis of Cross-reactivity in Children Allergic to Birch. Rocz Akad Med Bialymst. 2005;50:268-73. PubMed PMID: 16358981.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Immunoblotting in the diagnosis of cross-reactivity in children allergic to birch. AU - Cudowska,B, AU - Kaczmarski,M, AU - Restani,P, PY - 2005/12/20/pubmed PY - 2006/2/1/medline PY - 2005/12/20/entrez SP - 268 EP - 73 JF - Roczniki Akademii Medycznej w Bialymstoku (1995) JO - Rocz Akad Med Bialymst VL - 50 N2 - PURPOSE: The scientific experiments with new immunological methods (immunoblotting, RAST inhibition) and isolation of recombinant allergens suggest structural similarities in the allergenic components responsible for cross-reactions. Immunochemical and molecular biology studies indicate that epitopes of major allergen (Bet v 1, Mal d 1) contain more IgE binding epitopes than minor allergens (Bet v 2, Mal d 2), what explained clinical importance of major birch and apple allergens, but it is individual. The important role in cross-reactivity play also proteins with low molecular weight; a potentially dangerous allergen is lipid transfer protein (LTP) inducing severe systemic reactions in allergic subjects. The recent studies indicate that the IgE cross-reactivity patterns and the clinical relevance is still not clear and that only some of patients with confirmed IgE cross allergy to Bet v 1 and Mal d 1 demonstrated clinical symptoms after ingesting of apple. The aim of study was to establish the pattern of cross-reactivity between major (Bet v 1) and minor (Bet v 2) birch pollen allergens and apple proteins in children allergic to birch using recombinant allergens and immunoblotting method. MATERIAL AND METHODS: The prospective study were carried out on the group of 13 children aged 4-16 years, referred to the IIIrd Department of Paediatrics in Białystok and outpatient clinic with clinical symptoms of food and inhalant allergy. Inclusion criteria to the study were: allergy to birch pollen recombinant allergens and apple, confirmed by presence of specific IgE in the sera of patients. The allergens from peel and pulp of apple and birch were separated and loaded onto the polyacrylamide electrophoretic gel and than transferred to membranes by Western blotting. Antigen-IgE complex was detected using goat anti-human IgE antibodies labelled with alkaline phosphatase. RESULTS: Only few sera presented strong reactions in immunoblotting to birch pollen proteins with a molecular weight of 17-18 kDa, corresponding to the main birch allergen Bet v 1. Most of sera having positive reaction vs Bet v 1 showed cross-reactivity with Mal d 1. All sera recognized specifically the main allergen of apple peel Mal d 3 with molecular weight < 10 kDa (Lipid Transfer Protein). CONCLUSIONS: Immunoblotting method allows to verification of cross-reactivity recognized by presence of specific IgE. The nature of proteins responsible for sensitization can influence the spectrum of offending foods and the clinical features of allergic reactions. UR - https://www.unboundmedicine.com/medline/citation/16358981/Immunoblotting_in_the_diagnosis_of_cross_reactivity_in_children_allergic_to_birch_ L2 - https://air.unimi.it/handle/2434/6694 DB - PRIME DP - Unbound Medicine ER -