Demonstration of Close Physicochemical Similarity and Partial Immunochemical Identity between the Major Allergen, Dp42, of the House Dust Mite, &lt;i&gt;D. pteronyssinus&lt;/i&gt; and Corresponding Antigens of &lt;i&gt;D. farinae&lt;/i&gt; (Of 6) and &lt;i&gt;D. microceras&lt;/i&gt; (Dm6)

Lind, Peter

doi:10.1159/000233943

Cited by 50 publications

(21 citation statements)

References 7 publications

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“…These observations support the hypothesis that PK.3 protease is a D erf I allergen protein, since the D erf I group allergen is recognized to be a heat-labile glycoprotein [2]. It was pointed out recently [14] that Der I allergen was closely related to fecal particles. Der I allergen may be derived from digestive protease secreted from the gastrointestinal tract of the house dust mite.…”

Section: Protease Activity and Allergenic Activity In The Precipitatesupporting

confidence: 84%

Characterization of the Proteases in the Crude Mite Extract

Ino¹,

Ando²,

Haida

et al. 1989

Int Arch Allergy Immunol

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Characterization of the proteases was performed in the crude mite extract fractionated by Sephacryl S-200 gel filtration. Three peaks of protease activities were detected in the fractions. From the results of substrate specificity and susceptibility to the inhibitors, PK.1 protease (about 60 kD) is suggested to be a trypsin-like protease of mites. From the results of susceptibility to various agents, PK.2 (about 30 kD) and PK.3 (about 20 kD) proteases may be cysteine proteases, e.g., papain and cathepsin B. PK.3 protease existed in the precipitate of 60% ammonium sulfate fractionation. The data in the present study suggest the possibility that Dermatophagoides farinae I allergen might be a cysteine protease probably derived from the gastrointestinal tract of the house dust mite.

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Section: Protease Activity and Allergenic Activity In The Precipitatesupporting

confidence: 84%

Characterization of the Proteases in the Crude Mite Extract

Ino¹,

Ando²,

Haida

et al. 1989

Int Arch Allergy Immunol

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“…It is well documented that allergy to house dust is one major cause of asthma and rhinitis [26,27], More over, several antigens and allergens in the house dust mite genus Dermatophagoides have been character ized and isolated [14][15][28][29]. Allergy to stored farming material caused by different genera of stor age mites also seems to be of importance [3][4][5][10][11][12][13].…”

Section: Discussionmentioning

confidence: 99%

Demonstration of Allergen Components in the Storage Mite <i>Lepidoglyphus destructor</i> by an Immunoblotting Technique

Johansson

Hage‐Hamsten²,

Johansson³

1988

Int Arch Allergy Immunol

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The allergen composition of crude extracts of the storage mite Lepidoglyphus destructor were investigated by sodium dodecylsulphate polyacrylamide gel electrophoresis and immunoblotting. The allergen components were detected by sera from allergic farmers with a positive radioallergosorbent test to L. destructor. The allergen-antibody complexes were visualized by rabbit anti-IgE and β-galactosidase-labelled sheep antirabbit IgG in a chromogenic substrate. Six out of the forty-three sera also had IgE antibodies to the culture medium, which were neutralized by addition of medium antigens before the demonstration of mite allergen components. A total of 11 allergen components were identified. Two of them were found to be major allergen components, identified by more than 50% of the 43 sera used in the study. These 2 IgE-binding components had molecular weights of approximately 18,000 and 16,000 daltons, respectively.

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“…The Group I allergens (Derp I, Derf I, Der m I) are heat-labile glycoproteins (relative molecular mass, Mr, 25 000), which are heterogeneous on isoelectricfocusing (IEF) (pI, 4.7-7.4) and are excreted in faeces (5,9,10,27,(31)(32)(33). These allergens appear to be structural homologues and have very similar Nterminal amino acid sequences.…”

Section: Identification and Standardizationmentioning

confidence: 99%

Dust mite allergens and asthma—A worldwide problem

Platts‐Mills¹,

deWeck²,

Aalberse³

et al. 1989

Journal of Allergy and Clinical Immunology

597

304

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After the discovery ofhouse dust mites in 1964 their association with asthma has been reported from many different parts of the world including the developing countries. Two sets of major allergens from mites of the genus Dermatophagoides are now well recognized. The Group I allergens are glycoproteins of relative molecular mass (Mr) 25 000, which show both structural homology and cross-reactivity. The allergen Der p I has been cloned and sequenced confirming the M, and establishing its nature as a protease. The Group II allergens (Mr 15 000) show even closer homology and cross-reactivity.Specific immunoassays for Group I and Group II allergens, using monospecific antisera and monoclonal antibodies, have been standardized and are suitable for measuring allergen levels in different parts of the world.Measures for reducing the levels of mite allergens in houses include the covering of mattresses, hot washing of bedding, and removal of carpets from bedrooms as well as humidity control, vacuum cleaning, and the use ofacaricides in the rest ofthe house. There is already evidence that these procedures can cause a major improvement in the symptoms of asthma. While provisional standards for both sensitization to mites and also mite allergen exposure can now be recommended, there is an urgent needfor controlled studies using protocols demonstrated to reduce mite allergen levels by at least tenfold and for further international collaboration.

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Demonstration of Close Physicochemical Similarity and Partial Immunochemical Identity between the Major Allergen, Dp42, of the House Dust Mite, <i>D. pteronyssinus</i> and Corresponding Antigens of <i>D. farinae</i> (Of 6) and <i>D. microceras</i> (Dm6)

Cited by 50 publications

References 7 publications

Characterization of the Proteases in the Crude Mite Extract

Characterization of the Proteases in the Crude Mite Extract

Demonstration of Allergen Components in the Storage Mite <i>Lepidoglyphus destructor</i> by an Immunoblotting Technique

Dust mite allergens and asthma—A worldwide problem

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