LATEX ALLERGEN DATABASE

Two-dimensional (2-D) electrophoresis followed by immunoblotting and N -terminal protein microsequencing were used to characterize and identi fy the IgE-reactive proteins of Hevea latex that are the main cause of the latex type I allergy affecting especially health care workers and spina bifida children. This approach generated a comprehensive latex allergen database, which facilitated the integration of most of the la tex allergen data presented in the literature. The major latex allerge ns Hev b 1, Hev b 3, Hev b 6 and Hev b 7 have been localized on our 2- D maps. Moreover, we were able to identify six previously undescribed IgE-binding latex proteins, namely enolase, superoxide dismutase, prot easome subunit C5, malate dehydrogenase, triosephosphate isomerase and endochitinase. The generated latex 2-D maps will provide valuable inf ormation to develop strategies for the isolation of the novel IgE bind ing proteins in order to study the frequency of sensitization among bo th risk groups. Detailed knowledge of all proteins involved in latex a llergy will allow better diagnosis of latex allergy and to monitor the success of prevention strategies that are needed to reduce the high p revalence of latex allergy among both risk groups.