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

Abstract

The most relevant allergen of the storage mite Lepidoglyphus destructor (Lep d I) has been characterized. Lep d I is a monomer protein of 13273 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 substitutions in three of them. No potential N‐glycosylation site was revealed by peptide sequencing, The 125‐residue sequence of Lep d I shows approximately 40% identity (including the six cysteines) with the overlapping regions of group II allergens from the genus Dermatophagoides, which, however, do not share common allergenic epitopes with Lep d I.

Solution Structure of Der f 2, the Major Mite Allergen for Atopic Diseases

“…Their sequences are 88% identical (2,3), and their cross-reactivity was well confirmed (1). They are also homologous to the major allergen from the mite Lepidoglyphus destructor (4), which is important in farming environments. These proteins are 125-129 amino acid residues long and have three intramolecular disulfide bonds.…”

Allergen cross‐reactivity between house‐dust mites and other invertebrates

“…The amino-acid sequence homology of Der 2 and Lep d 2 is 43%. For Der p 2 and Tyr p 2, this ®gure is 41%; between Der f 2 and Tyr p 2, there is 43% sequence homology (81,82).…”

Mites in facilities for laboratory animals

“…Attention should be paid to proper cleaning practices and protection against mites. The allergens from the storage mite Lepidoglyphus destrutor, such as Lep d 1 and Lep d 2, have been purified and characterized, and a method for measuring allergens in dust samples has been developed (24)(25)(26)(27)(28). Furthermore, we need new commercial methods for measuring storage mite allergens in order to study comprehensively the possible role of mites in sensitizing laboratory animal workers.…”