BACKGROUND: The house dust mite Euroglyphus maynei inhabits homes in many parts of the world and is the source of many allergens. OBJECTIVE: The purpose of this study was to biochemically and immunologically characterize the major allergens of E. maynei. METHODS: Proteins in an extract of E. maynei were separated into 20 fractions by using preparative isoelectric focusing. Most proteins and allergens were contained in fractions 7 to 17 with pH of 4.8 to 8.0. The fractions were further characterized by nonreducing sodium dodecylsulfate-polyacrylamide gel electrophoresis and immunoblotting with the serum of 16 individuals sensitive to E. maynei. RESULTS: Molecular weights and isoelectric points were assigned to 47 IgE-binding proteins in an E. maynei extract, and the frequency of IgE binding to each allergen was determined. Twenty-two of the allergens were recognized by more than 50% of the 16 sera, and all but one of the subjects had IgE that bound to more than 10 allergens (range, 0 to 32). One of the proteins was identified as the allergen Eur m 2. CONCLUSION: E. maynei is the source of at least 47 individual allergens that have been characterized by molecular weight, isoelectric point, and IgE-binding properties.
BACKGROUND: The house dust mite Euroglyphus maynei inhabits homes in many parts of the world and is the source of many allergens. OBJECTIVE: The purpose of this study was to biochemically and immunologically characterize the major allergens of E. maynei. METHODS: Proteins in an extract of E. maynei were separated into 20 fractions by using preparative isoelectric focusing. Most proteins and allergens were contained in fractions 7 to 17 with pH of 4.8 to 8.0. The fractions were further characterized by nonreducing sodium dodecylsulfate-polyacrylamide gel electrophoresis and immunoblotting with the serum of 16 individuals sensitive to E. maynei. RESULTS: Molecular weights and isoelectric points were assigned to 47 IgE-binding proteins in an E. maynei extract, and the frequency of IgE binding to each allergen was determined. Twenty-two of the allergens were recognized by more than 50% of the 16 sera, and all but one of the subjects had IgE that bound to more than 10 allergens (range, 0 to 32). One of the proteins was identified as the allergen Eur m 2. CONCLUSION:E. maynei is the source of at least 47 individual allergens that have been characterized by molecular weight, isoelectric point, and IgE-binding properties.