A novel acidic allergen, Hev b 5, in latex. Purification, cloning and characterization

Abstract

Latex allergy is recognized as a serious health problem among health care workers and children with spina bifida. A number of IgE-reactive proteins have been identified in natural and processed latex products. One of the most acidic proteins in the cytoplasm of lacticifer cells of rubber trees (Hevea brasiliensis) is demonstrated to be a potent allergen in eliciting allergic reactions in humans. This protein, with pI = 3.5, has a molecular mass of 16 kDa with a blocked N terminus and an unusual amino acid composition. This acidic protein was found in extracts prepared from latex gloves, which were shown to be allergenic. The purified protein elicits histamine release from human basophils passively sensitized with serum from latex-allergic individuals in a dose-dependent manner. From a latex cDNA library, the cDNA coding for this protein was isolated and sequenced. The deduced amino acid sequence shows a high degree of homology to another acidic protein identified in kiwifruit (Actinidia deliciosa var. deliciosa). The sequence homology (47% sequence identity) between these two acidic proteins suggests a molecular explanation for the high frequency of fruit hypersensitivity in latex-allergic patients.