Demonstration of Allergen Components in the Storage Mite <i>Lepidoglyphus destructor</i> by an Immunoblotting Technique

Abstract

The allergen composition of crude extracts of the storage mite Lepidoglyphus destructor were investigated by sodium dodecylsulphate polyacrylamide gel electrophoresis and immunoblotting. The allergen components were detected by sera from allergic farmers with a positive radioallergosorbent test to L. destructor. The allergen-antibody complexes were visualized by rabbit anti-IgE and β-galactosidase-labelled sheep antirabbit IgG in a chromogenic substrate. Six out of the forty-three sera also had IgE antibodies to the culture medium, which were neutralized by addition of medium antigens before the demonstration of mite allergen components. A total of 11 allergen components were identified. Two of them were found to be major allergen components, identified by more than 50% of the 43 sera used in the study. These 2 IgE-binding components had molecular weights of approximately 18,000 and 16,000 daltons, respectively.

Purification and characterization of Lep d I, a major allergen from the mite Lepidoglyphus destructor

“…2), then causing a variation of the apparent MW from 14 kD (in the absence of ^-ME) to 16 kD. The latter value tallies with that reported for one of the two main allergenic components from L. destructor identified by other authors [7].…”

Quantitation of major allergens in dust samples from urban populations collected in different seasons in two climatic areas of the Basque region (Spain)

“…There is controversy (1,8,10,31) about the in vitro studies on cross-reactivity. In a recent study, Johansson et al (11) showed, through immunoblotting inhibition, that only two L. destructor minor components had some cross-reactivity with D. pteronyssinus.…”

Primary Structure of Lep D I, the Main Lepidoglyphus Destructor Allergen

“…Although several polypeptides with IgE-binding ability were identified in L. destructor extracts by SDSPAGE immunoblotting, a protein of approximately 14000 Da was demonstrated to be the principal allergen [9,101. In a previous work [ll], we purified this protein by mAb-based affinity chromatography, and showed that the protein preparation met the purity requirements of the International Union of Immunological Societies Sub-committee for Allergen Nomenclature to be termed Lep d I [12].…”