PRIMARY STRUCTURE OF LEP D I, THE MAIN LEPIDOGLYPHUS-DESTRUCTOR ALLERGEN

The most relevant allergen of the storage mite Lepidoglyphus destructo r (Lep d I) has been characterized. Lep d I is a monomer protein of 13 273 Da. The primary structure of Lep d I was determined by N-terminal Edman degradation and partially confirmed by cDNA sequencing. Sequence polymorphism was observed at six positions, with non-conservative sub stitutions in three of them. No potential N-glycosylation site was rev ealed by peptide sequencing. The 125-residue sequence of Lep d I shows approximately 40% identity (including the six cysteines) with the ove rlapping regions of group II allergens from the genus Dermatophagoides , which, however, do not share common allergenic epitopes with Lep d I .