Literature DB >> 2180541

Recent progress in mite allergen immunochemistry.

P W Heymann1, M D Chapman.   

Abstract

The successful purification of several mite allergens within the last few years has considerably enhanced our understanding of mite allergen immunochemistry. The role of these glycoproteins in stimulating human IgE ab and their role as immunogens in mice and rabbits has been studied extensively in a number of laboratories worldwide. In particular, purified allergens have facilitated the production of murine IgG Mabs that have been used to purify mite allergens by affinity chromatography; to investigate the diversity of antigenic sites on purified allergens; and to develop Mab based immunoassays for measuring allergen concentrations in dust samples and extracts. Full amino acid sequencing of several mite allergens is now in progress together with efforts to identify antigenically important peptide fragments. Such investigations are aimed to further increase our knowledge of humoral and cellular immune responses at the molecular level. For years, pollen counts have been used to judge airborne pollen allergen levels and to predict, in turn, the severity of symptom days for patients with hay fever. In contrast, simple methods for measuring dust allergens (e.g., mite allergen) have not been available. The development of Mab immunoassays, which can be converted from radiolabeled to enzyme labeled or fluorescence labeled assays, should provide rapid and quantitative measurements of specific mite allergen levels in house dust. Not only can such measurements provide useful clinical information in judging the exposure of patients to mite allergen, but the effectiveness of allergen avoidance regimes can be monitored objectively. By measuring the concentration of specific allergens in extracts, these assays could significantly improve efforts to standardize extracts used for diagnosis and treatment.

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Year:  1990        PMID: 2180541     DOI: 10.1007/BF02914436

Source DB:  PubMed          Journal:  Clin Rev Allergy        ISSN: 0731-8235


  47 in total

Review 1.  House dust mites.

Authors:  G W Wharton
Journal:  J Med Entomol       Date:  1976-02-20       Impact factor: 2.278

2.  Antigen Der f I from the dust mite Dermatophagoides farinae: structural comparison with Der p I from Dermatophagoides pteronyssinus and epitope specificity of murine IgG and human IgE antibodies.

Authors:  P W Heymann; M D Chapman; T A Platts-Mills
Journal:  J Immunol       Date:  1986-11-01       Impact factor: 5.422

3.  Pyroglyphid mites (Acari) and house dust allergy.

Authors:  J E van Bronswijk; R N Sinha
Journal:  J Allergy       Date:  1971-01

4.  Allergen nomenclature.

Authors:  D G Marsh; L Goodfriend; T P King; H Lowenstein; T A Platts-Mills
Journal:  Bull World Health Organ       Date:  1986       Impact factor: 9.408

5.  Mites and asthma in children.

Authors:  J O Warner
Journal:  Br J Dis Chest       Date:  1978-04

6.  Isolation and characterization of the allergen Dpt 12 from Dermatophagoides pteronyssinus by chromatofocusing.

Authors:  G A Stewart
Journal:  Int Arch Allergy Appl Immunol       Date:  1982

7.  Monoclonal immunoassays for major dust mite (Dermatophagoides) allergens, Der p I and Der f I, and quantitative analysis of the allergen content of mite and house dust extracts.

Authors:  M D Chapman; P W Heymann; S R Wilkins; M J Brown; T A Platts-Mills
Journal:  J Allergy Clin Immunol       Date:  1987-08       Impact factor: 10.793

8.  Clinical significance of skin reactions to mite extracts in children with asthma.

Authors:  J M Smith; M E Disney; J D Williams; Z A Goels
Journal:  Br Med J       Date:  1969-06-21

9.  Demonstration of close physicochemical similarity and partial immunochemical identity between the major allergen, Dp42, of the house dust mite, D. pteronyssinus and corresponding antigens of D. farinae (Df6) and D. microceras (Dm6).

Authors:  P Lind
Journal:  Int Arch Allergy Appl Immunol       Date:  1986

10.  Isolation and characterization of the main allergen of Dermatophagoides farinae by monoclonal antibodies that recognize IgE related epitopes.

Authors:  V Ley; J C Sáiz; J Carreira
Journal:  Mol Immunol       Date:  1986-12       Impact factor: 4.407

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