Characterization of the allergens of the house dust mite Euroglyphus maynei.
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.


CONCLUSIONS
E. maynei is the source of at least 47 individual allergens that have been characterized by molecular weight, isoelectric point, and IgE-binding properties.
Morgan
M S
MS
Department of Biological Sciences, Wright State University, Dayton, Ohio 45435, USA.
Arlian
L G
LG
Barnes
K C
KC
Fernandez-Caldas
E
E
D000485:Allergens / Q000737:chemistry* / Q000276:immunology; D000818:Animals; D004391:Dust; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D015151:Immunoblotting; D007073:Immunoglobulin E / Q000097:blood / Q000378:metabolism; D007526:Isoelectric Point; D008925:Mites / Q000276:immunology*; D008970:Molecular Weight; D011480:Protease Inhibitors / Q000494:pharmacology
D000485:Allergens; D004391:Dust; D011480:Protease Inhibitors; D007073:Immunoglobulin E