Altered antigenicity of M‐177, a 177‐kDa allergen from the house dust mite Dermatophagoides farinae, in stored extract | Semantic Scholar (2024)

This work cloned a novel high mw Dermatophagoides pteronyssinus (Dp) mite allergen, Der p 11, which is regarded as important indoor allergens.

The aims of this study were to clone the cDNA of Der f 14 corresponding to M-177 and to elucidate the allergenic capacities of the N-terminal fragment of Derf 14 (Der f 14-N), and to show the highest capacity to induce cell proliferation in murine lymphocyte and human peripheral mononuclear cells among Der f 13-derived fragments.

The IgE response of humans to Der f 18 has been investigated and there is no report on Der f 15‐specific IgE in humans, but in dogs the main IgE binding is directed to the D. farinae chitinase allergens.

The full IgE‐binding spectrum of C. japonica pollen allergens demonstrates that many allergens remain to be identified.

Immunoblotting and ELISA tests showed that the isolated peptide strongly cross-reacted with the IgE of patients, thus classifying it as a significant allergen.

It is timely to discuss not only paramyosin but also some emerging features of the spectrum of allergens produced by Dermatophagoides mites, which have largely eluded the recent progress in the characterization of mite allergens.

The results of immunoblotting studies of the allergens in extracts of the mites have differed in detail, but the broad picture shows both complexity and the existence of some dominant specificities, which should be recognized.

The native Blo t 11 allergen from Blomia tropicalis was isolated and compared with the recombinant forms to compare its aller Genetically modified forms.

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A cDNA clone encoding a new allergen from the Dermatophagoides farinae cDNA lambda gt11 library was isolated and sequenced and had a potent ability to release histamine from washed blood cells of the mite-allergic patients.

A lambda gt11 library made with cDNA from the house dust mite Dermatophagoides pteronyssinus was screened with human allergic serum by IgE plaque radioimmunoassay, resulting in the isolation of clones coding for the major allergen Der p II, which resulted in the cloning of the two major mite allergens.

Affinity purification of rabbit antibodies with the clone showed that antibodies to the polypeptide had specificities to multiple products in mite extracts corresponding to components of Mr 29, 27 and 24 K by Western blotting.

Nearly all antigens detected by CIE could be identified as allergens using CRIE, and proteins of higher molecular weights showed IgE-binding capacities.

The engineered allergen, in which the disulfide bond that linked the N- and C-terminal sequences of Der f 2 was disrupted, retained T- cell epitopes essential for immunotherapy and ability to stimulate T-cell proliferation.

The electroblotting procedure employing specific probes, using mite-allergic human sera as the first antibody source, promises to be a valuable aid for allergen standardization.

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