+ Site Statistics
References:
54,258,434
Abstracts:
29,560,870
PMIDs:
28,072,757
+ Search Articles
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ PDF Full Text
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Translate
+ Recently Requested

Major house dust mite allergens Dermatophagoides pteronyssinus 1 and Dermatophagoides farinae 1 degrade and inactivate lung surfactant proteins A and D



Major house dust mite allergens Dermatophagoides pteronyssinus 1 and Dermatophagoides farinae 1 degrade and inactivate lung surfactant proteins A and D



Journal of Biological Chemistry 282(51): 36808-36819



Lung surfactant proteins (SP) A and D are calcium-dependent carbohydrate-binding proteins. In addition to playing multiple roles in innate immune defense such as bacterial aggregation and modulation of leukocyte function, SP-A and SP-D have also been implicated in the allergic response. They interact with a wide range of inhaled allergens, competing with their binding to cell-sequestered IgE resulting in inhibition of mast cell degranulation, and exogenous administration of SP-A and SP-D diminishes allergic hypersensitivity in vivo. House dust mite allergens are a major cause of allergic asthma in the western world, and here we confirm the interaction of SP-A and SP-D with two major mite allergens, Dermatophagoides pteronyssinus 1 and Dermatophagoides farinae 1, and show that the cysteine protease activity of these allergens results in the degradation of SP-A and SP-D under physiological conditions, with multiple sites of cleavage. A recombinant fragment of SP-D that is effective in diminishing allergic hypersensitivity in mouse models of dust mite allergy was more susceptible to degradation than the native full-length protein. Degradation was enhanced in the absence of calcium, with different sites of cleavage, indicating that the calcium associated with SP-A and SP-D influences accessibility to the allergens. Degradation of SP-A and SP-D was associated with diminished binding to carbohydrates and to D. pteronyssinus 1 itself and diminished capacity to agglutinate bacteria. Thus, the degradation and consequent inactivation of SP-A and SP-D may be a novel mechanism to account for the potent allergenicity of these common dust mite allergens.

(PDF emailed within 0-6 h: $19.90)

Accession: 019364633

Download citation: RISBibTeXText

PMID: 17848554

DOI: 10.1074/jbc.m702336200


Related references

Elisa for determination of major excrement allergens of house dust mite species dermatophagoides pteronyssinus dermatophagoides farinae and dermatophagoides microceras. Allergy 41(6): 442-451, 1986

Absence of continuous epitopes in the house dust mite major allergens Der p I from Dermatophagoides pteronyssinus and Der f I from Dermatophagoides farinae. Clinical and Experimental Allergy 26(1): 36-42, 1996

Demonstration of close physicochemical similarity and partial immunochemical identity between the major allergen dp 42 of the house dust mite dermatophagoides pteronyssinus and corresponding antigens of dermatophagoides farinae df 6 and dermatophagoides microceras dm 6. International Archives of Allergy & Applied Immunology 79(1): 60-65, 1985

Immune reactivity of recombinant group 2 allergens of house dust mite, Dermatophagoides pteronyssinus, and Dermatophagoides farinae. Journal of Investigational Allergology & Clinical Immunology 13(1): 36-42, 2003

Identification of major allergens from the house dust mites, Dermatophagoides farinae and Dermatophagoides pteronyssinus, by electroblotting. Yonsei Medical Journal 32(1): 24-32, 1991

Cross reacting and species specific determinants on a major allergen from dermatophagoides pteronyssinus and dermatophagoides farinae development of a radioimmunoassay for antigen p 1 equivalent in house dust and dust mite extracts. Journal of Allergy & Clinical Immunology 78(3 PART 1): 398-407, 1986

Reactivity to intradermal injection of extracts of Dermatophagoides farinae, Dermatophagoides pteronyssinus, house dust mite mix, and house dust in dogs suspected to have atopic dermatitis: 115 cases (1996-1998). Journal of the American Veterinary Medical Association 217(4): 536-540, 2000

Mites and house dust allergy. II. Relationship between house dust and mite (Dermatophagoides pteronyssinus and D. farinae) allergens by fractionation methods. Clinical Allergy 2(2): 115-123, 1972

House dust mite (Dermatophagoides farinae and Dermatophagoides pteronyssinus) prevalence in the rooms and hallways of a tertiary care hospital. Journal of Allergy and Clinical Immunology 95(4): 801-805, 1995

The stability of aqueous and glycerinated house dust mite extracts dermatophagoides pteronyssinus and dermatophagoides farinae as measured by rast inhibition. Journal of Allergy & Clinical Immunology 85(1 PART 2): 238, 1990

Enzymatic analyses of house dust mite extracts from Dermatophagoides pteronyssinus and Dermatophagoides farinae (Acari: Pyroglyphidae) during different phases of culture growth. Journal of Medical Entomology 36(3): 370-375, 1999

The early changes of Dermatophagoides farinae -specific IgE, IgG1, and IgG4 after rush immunotherapy with Df and Dermatophagoides pteronyssinus in house dust mite sensitive asthma. Journal of Allergy & Clinical Immunology 107(2): S255, 2001

Intradermal skin testing with Dermatophagoides pteronyssinus and Dermatophagoides farinae in a southern United States area where DP is the predominate house dust mite. Journal of Allergy & Clinical Immunology 99(1 PART 2): S346, 1997

Purification and partial characterization of two major allergens from the house dust mite Dermatophagoides pteronyssinus. Journal of Allergy and Clinical Immunology 76(5): 753-761, 1985

T cell responses to the purified major allergens from the house dust mite Dermatophagoides pteronyssinus. Journal of Allergy and Clinical Immunology 89(5): 1021-1031, 1992