Background: There is general agreement that proteins eluting from different natural rubber latex products can cause immediate type hypersensitivity reactions in latex-allergic patients. However, there is as yet no consensus as to what are the most important allergens in natural rubber latex.
Objective: We wanted to purify and characterize at the primary structure level three natural latex proteins, suggested to represent significant allergens.
Methods: Proteins were purified from ultracentrifuged bottom fraction of natural rubber latex using high performance liquid chromatography gel filtration and reversed phase chromatography. Purified proteins were subjected to tryptic cleavage, peptide separation and amino acid sequencing. Immunoblotting was used to demonstrate IgE antibodies to the purified proteins in sera from latex-allergic patients.
Results: A 20 kDa protein was identified by amino acid sequencing as prohevein, a major protein in the rubber tree Hevea brasiliensis, and a 30 kDa natural rubber latex protein as hevamine, another essential rubber tree protein. A third, previously undescribed natural rubber latex protein, showed high homology to several plant endo-1,3-beta-glucosidases. In immunoblotting, the purified prohevein bound IgE antibodies from 24/29 (83%) sera of latex-allergic patients including positive results in 4/6 latex-allergic children with spina bifida or other congenital anomalies. The purified prohevein elicited positive skin-prick test reactions in all six latex-allergic patients showing IgE to prohevein. The purified 36 kDa protein bound IgE from 6/29 (21%) latex-allergic sera, and the purified hevamine from only 1/29 patient sera.
Conclusion: The observed high frequency of IgE antibodies to prohevein suggests that this protein is a major natural rubber latex allergen.