A comparative study of three serine proteases from Dermatophagoides pteronyssinus and D. farinae.

Studies have shown that the dust mites Dermatophagoides pteronyssinus and D. farinae contain several serine proteases, two of which have been shown to be allergenic, and to include trypsin and chymotrypsin, corresponding to the groups III and VI mite allergens. However, mites also contain other serine proteases, and the data reported in this study show that an elastase-like enzyme is present in both species. This enzyme was differentiated from the other serine proteases, particularly chymotrypsin, on the basis of charge, substrate specificity, and inhibition by copper and mercury cations. Its apparent mol. mass, as judged by gel filtration, was similar to those previously described for trypsin and chymotrypsin, i.e., 30 kDa. Several isoforms were detected by isoelectric focusing, but the isoelectric points of the major forms in both D. pteronyssinus and D. farinae were 10.5 and 9.8, respectively, contrasting with the acidic mite chymotrypsins. All three serine proteases were detected in whole mite and faecally enriched extracts, but the activities of trypsin and the elastase-like enzyme were greater in the latter type of extract. These data were similar to those obtained by quantitative immunochemical analysis of the D. farinae group III allergen in appropriate extracts, suggesting that culture conditions may modulate protease production. A monoclonal antibody affinity matrix specific for the group III allergen from D. farinae was shown to bind mite trypsin. However, a small amount of mite chymotrypsin also bound, suggesting limited immunologic cross-reactivity, a finding consistent with known sequence data.

Immunobiology of the serine protease allergens from house dust mites.

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.