To support its ongoing monitoring program of therapeutic and diagnostic allergen preparations, LAIB has initiated a multifaceted study of the relationship between the structure and function of allergens. These include: 1. Physical identification of allergens. We have initiated studies on the use of HPLC and MALD-TOF techniques, and microarray analyses, in the characterization of target allergens. 2. Role of glycosylation in allergen recognition and processing. Recent advances in the bioengineering and cloning of allergens have raised new questions about the immunogenicity of non-glycosylated proteins. Dr. Soldatova has studied the role of glycosylation in the immunogenicity of recombinant bee venom hyaluronidase. Using the model of site-specific mutagenesis of these and other recombinant proteins, we will expand our current studies in this area. 3. Enzyme activity as a measure of allergenicity. Current standards require the presence of active hyaluronidase and phospholipase in venom extracts. We have initiated studies to address the issue of the relevance of these activities for allergenicity. Publications: Superior Biological Activity of the Recombinant Bee Venom Allergen Hyaluronidase Express in Baculovirus-Infected Insect Cells as Compared With Escherichia coli, Soldatova L.N., Crameri R., Gmaci M., Kemeny D.M., Schmidt M., Weber M, Mueller U.R., Journal of Allergy and Clinical Immunology, 1998; 101:691-698.
