Allergen Source Materials and Quality Control of Allergenic Extracts

Esch, Robert E.

doi:10.1006/meth.1997.0491

Cited by 62 publications

(47 citation statements)

References 19 publications

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“…The commercially available natural extracts also show variation from one manufacturer to another, may be due to source material of different batches and location or method of preparation (Esch, 1997). Recombinant proteins are homogenous preparations with defined allergenic potency that show promise for component resolved diagnosis and therapy of allergic diseases (Wiedermann, 2005).…”

Section: Discussionmentioning

confidence: 99%

Molecular and immunological characterization of subtilisin like serine protease, a major allergen of Curvularia lunata

et al. 2011

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Section: Discussionmentioning

confidence: 99%

Molecular and immunological characterization of subtilisin like serine protease, a major allergen of Curvularia lunata

et al. 2011

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“…The quality of the extracts is influenced by many factors including quality of the starting raw material [7], extraction procedure [8], protease content [9]and storage conditions [10]. These factors strongly influence the final composition, potency and stability of allergen preparations and, as a consequence thereof, the outcome of diagnostic tests in vitro [11]and in vivo [12].…”

Section: Use Of Crude Allergens or Allergen Extracts For Skin Testingmentioning

confidence: 99%

Recombinant Allergens for Skin Testing

Schmid‐Grendelmeier¹,

Crameri²

2001

Int Arch Allergy Immunol

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Skin testing is a basic diagnostic procedure widely used to explore immediate-type reactions to allergen preparations in vivo. Despite their reliability, if standardized extracts are used, skin tests suffer from limited reproducibility due to difficulties in preparing consistently standardized extracts from natural raw material. Starting from allergen-encoding cDNAs, large amounts of highly pure allergens with a high batch-to-batch consistency satisfying the quality requirements of medicinal products manufactured by recombinant DNA technology can be produced. These reagents are expected to be qualitatively superior to the commercially available allergen preparations used for the in vitro and in vivo diagnosis of allergic conditions. In this article the current literature available on skin testing with such recombinant allergens (rAllergens) is reviewed and critically analyzed. To date many different rAllergens of various pollens, moulds, mites, bee venom, latex and celery have been used in skin testing in more than 1,600 allergic and control individuals. Skin prick tests as well as intradermal skin tests with rAllergens prove to be highly specific and safe. The diagnostic sensitivity of single rAllergens is generally lower than those obtained with allergen extracts, but can be considerably increased by using rAllergen panels covering the most important allergenic structures present in a given complex allergenic extract. Moreover, quantitative skin testing with single rAllergens allows interesting insights into correlations between the in vivo and in vitro sensitization to a given allergen. In conclusion, skin testing with rAllergens offers a highly specific and safe additional diagnostic tool to elucidate patient- and disease-specific sensitization patterns which will be needed for the development of patient-tailored immunotherapeutic treatments.

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“…However, major problems in the preparation of HDM allergen extracts are due to the fact that these extracts contain several different important allergens and several proteases which may lead to degradation, and the allergen composition varies depending on culture conditions, source material (mite bodies and mite cultures), extraction procedures and storage conditions [17,18,19,20]. A recent study indicated that there is considerable variation of the major HDM allergens, Der p 1 and Der p 2 in commercial D. pteronyssinus extracts, but there are no data available regarding other important HDM allergens [21].…”

Section: Introductionmentioning

confidence: 99%

Varying Allergen Composition and Content Affects the in vivo Allergenic Activity of Commercial <b><i>Dermatophagoides pteronyssinus</i></b> Extracts

Casset¹,

Mari

Purohit

et al. 2012

Int Arch Allergy Immunol

159

112

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Background: Diagnosis and immunotherapy of house-dust mite (HDM) allergy is still based on natural allergen extracts. The aim of this study was to analyze commercially available Dermatophagoides pteronyssinus extracts from different manufacturers regarding allergen composition and content and whether variations may affect their allergenic activity. Methods: Antibodies specific for several D. pteronyssinus allergens (Der p 1, 2, 5, 7, 10 and 21) were used to analyze extracts from 10 different manufacturers by immunoblotting. Sandwich ELISAs were used to quantify Der p 1 and Der p 2 in the extracts. Mite-allergic patients (n = 45) were skin-tested with the extracts and tested for immunoglobulin E (IgE) reactivity to a panel of 10 mite allergens (Der p 1, 2, 4, 5, 7, 8, 10, 14, 20 and 21) by dot blot. Results: Only Der p 1 and Der p 2 were detected in all extracts but their concentrations and ratios showed high variability (Der p 1: 6.0–40.8 µg ml^–1; Der p 2: 1.7–45.0 µg ml^–1). At least 1 out of 4 allergens (i.e. Der p 5, 7, 10 and 21) was not detected in 8 of the studied extracts. Mite-allergic subjects showed different IgE reactivity profiles to the individual mite allergens, the extracts showed different allergenic activity in skin-prick tests and false-negative results. Conclusions: Commercially available D. pteronyssinus extracts lack important allergens, show great variability regarding allergen composition and content and some gave false-negative diagnostic test results in certain patients.

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Allergen Source Materials and Quality Control of Allergenic Extracts

Cited by 62 publications

References 19 publications

Molecular and immunological characterization of subtilisin like serine protease, a major allergen of Curvularia lunata

Molecular and immunological characterization of subtilisin like serine protease, a major allergen of Curvularia lunata

Recombinant Allergens for Skin Testing

Varying Allergen Composition and Content Affects the in vivo Allergenic Activity of Commercial <b><i>Dermatophagoides pteronyssinus</i></b> Extracts

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