β-Lactam drug allergens: Fine structural recognition patterns of cephalosporin-reactive IgE antibodies
✍ Scribed by Nghia H. Pham; Brian A. Baldo
- Publisher
- John Wiley and Sons
- Year
- 1996
- Tongue
- English
- Weight
- 775 KB
- Volume
- 9
- Category
- Article
- ISSN
- 0952-3499
No coin nor oath required. For personal study only.
✦ Synopsis
Lack of experimental findings on the spectrum of cephalosporin allergenic determinants has hindered diagnosis of adverse reactions to these drugs and retarded understanding of allergenic cross-reactions between cephalosporins and between cephalosporins and penicillins. Subjects allergic to the widely used cephalosporin antibiotic cefaclor have serum immuno globulin (Ig) E antibodies that react with the drug. Quantitative hapten inhibition studies employing sera from subjects allergic to cefaclor revealed fine structual recognition differences between the combining site specificities of cefaclor-reactive IgE antibodies in the sera of different subjects. Unlike penicillins, where discrete side chain or thiazolidine ring determinants alone may be recognized, IgE binding determinants on cefaclor encompassed the entire molecule. Fine structural recognition specificity differences at positions R, (side-chain) and R2 (substituent attached to dihydrothiazine ring) were detected between IgE antibodies in Merent sera. Some antibodies showed clear preferential recognition of the aminobenzyl group at position R, and C1 at R2 while with others, a greater degree of recognition tolerance was seen at R, where, for example, the aminohydroxybenzyl or aminodihydrobenzyl groups were recognized, and at R2 where a methyl or even an ester group was tolerated. As with the penicillins, cephalosporins as allergens cannot simply be considered as a group of compounds with a common allergenic determinant structure. IgE antibodies that bind to cefaclor show great heterogeneity indicated by clear, fine structural differences in recognition of the R, and R, groups on the drug.