Primary structure of Lep d I, the main Lepidoglyphus destructor allergen.
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.
Varela
J
J
Research Department, Alergia e Inmunología Abelló S. A., Madrid, Spain.
Ventas
P
P
Carreira
J
J
Barbas
J A
JA
Gimenez-Gallego
G
G
Polo
F
F
D000485:Allergens / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002851:Chromatography, High Pressure Liquid; D017124:Conserved Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D013058:Mass Spectrometry; D008925:Mites / Q000276:immunology*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D014176:Protein Biosynthesis; D011506:Proteins / Q000737:chemistry* / Q000302:isolation & purification; D016364:Reading Frames; D017386:Sequence Homology, Amino Acid
D000485:Allergens; C090039:Lep d I allergen; D011506:Proteins