ALLERGY TO BOVINE BETA-LACTOGLOBULIN - SPECIFICITY OF HUMAN IGE USINGCYANOGEN BROMIDE-DERIVED PEPTIDES

Citation
I. Selo et al., ALLERGY TO BOVINE BETA-LACTOGLOBULIN - SPECIFICITY OF HUMAN IGE USINGCYANOGEN BROMIDE-DERIVED PEPTIDES, International archives of allergy and immunology, 117(1), 1998, pp. 20-28
Citations number
28
Categorie Soggetti
Allergy,Immunology
ISSN journal
10182438
Volume
117
Issue
1
Year of publication
1998
Pages
20 - 28
Database
ISI
SICI code
1018-2438(1998)117:1<20:ATBB-S>2.0.ZU;2-M
Abstract
Background: Bovine beta-Lactoglobulin (Blg) is a major allergen involv ed in allergy to cow's milli proteins. Hydrolyzing Big did not totally suppress its allergenicity; moreover its immunoreactivity may be incr eased. The aim of this work was to evaluate the specificity of serum I gE to different fragments of Big in a group of 19 individuals allergic to cow's milk. Methods: This study was performed using both direct an d competitive inhibition ELISA involving immobilized native protein or peptides derived from Blg cyanogen bromide cleavage. Results: Analyse s of responses to each peptide revealed a large number of epitopes rec ognized by specific IgE of human allergic sera. However, there were di fferences in the specific determinants recognized, depending on the se rum. Generally, peptides (25-107) and (108-145) retained substantial p roportions of the immunoreactivity of the whole protein. Two other pep tides, i.e, (8-24) and (146-162), were less recognized but were not in ert. Conclusion: The main conclusion is that many epitopes were identi fied all along the Big sequence by specific anti-Big IgE from allergic humans.