Abstract
IgE-mediated allergy to proteins present in natural rubber latex is a well-recognized problem. Latex contains a complex mixture of proteins ranging in molecular weight from 6 to > 200 kD. The aim of this study was to determine whether shared allergenic sites exist on separate latex components. Following electrophoresis, latex components at 14, 24, and 46 kD were electroeluted from SDS-polyacrylamide gels and used in ELISA inhibition and immunoblot inhibition studies of human latex-specific IgE antibodies. A minimum of 4 major allergenic sites (for convenience labeled A through D) were found to exist in 3 components of nonammoniated latex. Minimally, 2 are present in the 14-kD component (A, B) and 3 in the 24-kD component (A-C). The 46-kD fraction has 3 or more antigenic sites (A, C, D) but lacks one (B) that is present in both the 14- and 24-kD components. Four different IgE-binding moieties were detected among three latex protein components (14, 24 and 46 kD). Some of these allergenic sites were shared by two or more components. Recovery of these and others from fragmented latex components will allow identification of their amino acid composition and their availability will ultimately lead to better diagnostic and therapeutic options for patients with latex allergy.
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