Molecular basis of IgE cross-reactivity between human β-casein and bovine β-casein, a major allergen of milk

被引:32
作者
Bernard, H
Negroni, L
Chatel, JM
Clement, G
Adel-Patient, K
Peltre, G
Creminon, C
Wal, JM
机构
[1] INRA, Lab Immunoallergie Alimentaire, F-91191 Gif Sur Yvette, France
[2] CEA Saclay, Serv Pharmacol & Immunol, F-91191 Gif Sur Yvette, France
[3] Inst Pasteur, Unite Immunoallergie, F-75724 Paris, France
关键词
cow's milk allergy; beta-casein; human milk; IgE; cross-reactivity;
D O I
10.1016/S0161-5890(00)00029-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Twenty patients allergic to cow's milk proteins and with high levels of specific IgE directed against bovine whole casein were selected to evaluate reactivity of their IgE antibodies with human beta-casein. Highly purified human and bovine beta-caseins were prepared by selective precipitations and FPLC separation. Their identity and purity were assessed by HPLC, analysis of amino acid composition, sequencing of the five N-terminal amino acid residues and immunochemical tests. Direct and indirect ELISAs were performed using human and bovine beta-casein coated into microtiter plates and monoclonal anti-human IgE antibody AChE labelled for revelation. Seven sera contained specific IgE directed against human beta-casein. Inhibition studies using native human and bovine beta-caseins as well as bovine beta-casein-derived peptides demonstrated that, depending on the sera, one or several common epitopes located in different parts of the molecule were shared by the two homologous proteins. (C) 2000 Elsevier Science Ltd. All rights reserved.
引用
收藏
页码:161 / 167
页数:7
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