IgE reactivity to α1 and α2 chains of bovine type I collagen in children with bovine gelatin allergy

JOURNAL OF ALLERGY AND CLINICAL IMMUNOLOGY

卷:104

Article

Sakaguchi, M ; Hori, H ; Hattori, S ; Irie, S ; Imai, A ; Yanagida, M ; Miyazawa, H ; Toda, M ; Inouye, S

关键词: allergen;    anaphylaxis;    cross-reactivity;    IgE;    gelatin;    vaccine;   

DOI  :  10.1016/S0091-6749(99)70344-1

来源: Elsevier

【 摘 要 】

Background: Anaphylactic reactions to measles, mumps, and rubella vaccines, including gelatin as a stabilizer, have been reported. It had been found that most of these reactions to live vaccines are caused by the bovine gelatin included in these vaccines. Gelatin mainly includes denatured type I collagen, which consists of alpha 1 and alpha 2 chains. Objective: The current study was designed to investigate the IgE reactivity to alpha 1 and alpha 2 chains of bovine type I collagen in gelatin-sensitive children. Methods: Serum samples were taken from 10 children who had anaphylaxis to the vaccines and high levels of specific IgE to bovine gelatin. Bovine type I collagen was isolated from bovine skin and then separated to alpha 1 and alpha 2 chains by column chromatography, IgE reactivity to denatured type I collagen and its alpha 1 and alpha 2 chains was analyzed by immunoblotting, ELISA, and histamine release from the mast cells passive sensitized with IgE antibodies in pooled serum of the children. Results: All children had specific IgE to bovine type I collagen. Furthermore, IgE antibodies in their sera reacted with the alpha 2 chain but not with the alpha 1 chain. Similarly, the mast cells sensitized with pooled sera in the children showed alpha 2 chain-specific histamine release but not a1 chain-specific histamine release. Conclusion: In gelatin allergy denatured bovine type I collagen is a major allergen and IgE-binding sites exist in the alpha 2 chain of type I collagen.

【 授权许可】

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