The presence of the enzymatically active allergens equivalent to Der p I (cysteine protease), Der p III (serine protease) and amylase in extracts of Dermatophagoides pteronyssinus, D. farinae and Euroglyphus maynei was determined using appropriate enzymatic techniques. Biochemical equivalents of all three allergens were present in each extract studied. Studies also showed that the mite extracts contained a variety of other biochemically active enzymes including trypsin, chymotrypsin, carboxypeptidase A and B, glucoamylase and lysozyme. Marked differences in the relative concentrations of some of these enzymes in different mite extracts were observed, particularly trypsin and carboxypeptidase A. The enzymes were physicochemically similar to equivalent enzymes from vertebrate and invertebrate sources. Chromatofocusing studies of faecal extracts derived from D. pteronyssinus and D. farinae showed that several isoforms of each enzyme were present. The data indicated that there were more trypsin isoforms, with pI over a wider range, in extracts prepared from D. pteronyssinus. Proteases and carbohydrases were also found in extracts prepared from faecally enriched material suggesting that they were endoperitrophic and associated with mite digestion. The data suggest that not only are the group I, III and amylase allergens a consistent feature of most pyroglyphid dust mites but also that other proteases and carbohydrases present in mite faeces are allergenic.
Extracts of Dermatophagoides pteronyssinus and D. farinae were shown to contain a variety of 30 kDa serine proteases, including trypsin, chymotrypsin, and an elastase-like enzyme. The mite trypsin, unlike chymotrypsin and the elastase enzyme, was heterogeneous with regard to charge. The enzymes were shown to be present at higher concentration in fecally enriched extracts than in whole mite extracts. The proteases were shown to induce vascular permeability and to detach cells in tissue culture. Further study showed that the mite elastase induced non-IgE mediated rat mast cell degranulation. Such properties may contribute to immunogenicity.
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