Purification and characterisation of relevant natural and recombinant apple allergens

Oberhuber, Christina; Ma, Yan; Marsh, Justin; Rigby, Neil M.; Smole, Ursula; Radauer, Christian; Alessandri, Stefano; Briza, Peter; Zuidmeer, Laurian; Maderegger, Bernhard; Himly, Martin; Sancho, Ana I.; Ree, Ronald van; Knulst, André C.; Ebner, Christof; Shewry, Peter R.; Mills, E. N. Clare; Wellner, Nikolaus; Breiteneder, Heimo; Hoffmann‐Sommergruber, Karin; Bublin, Merima

doi:10.1002/mnfr.200700522

Cited by 27 publications

(43 citation statements)

References 44 publications

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“…Yet, in 1999, Son et al [33], using cDNA of Mal d 1 from various apple strains amplified by a PCR strategy, found 12 Mal d 1 clones that were sequenced from 7 apple varieties and concluded that the divergent allergenicity of apple strains mainly depends on different expression levels of the major allergen. Second, allergens other than Mal d 1 may be relevant in inducing allergic symptoms to apple but may not be concerned with the effects of birch pollen IT; this is true for Mal d 2, a thaumatin-like protein, and Mal d 3, a lipid transfer protein [24,34], the latter showing around 100-fold differences in its levels between different apple cultivars [35]. In the present study, a role for such allergens was excluded on the basis of the negative results of the microarray test.…”

Section: Discussionmentioning

confidence: 99%

Birch-Apple Syndrome Treated with Birch Pollen Immunotherapy

Melato¹,

Russello²,

Incorvaia³

et al. 2011

Int Arch Allergy Immunol

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Background: The most common pollen-fruit cross-reaction is the birch-apple syndrome. Allergen immunotherapy (IT) is clearly effective for birch allergy, but its efficacy on apple allergy is controversial. We performed a randomized study on patients with birch-apple syndrome to evaluate the outcome of subcutaneous immunotherapy (SCIT) and sublingual immunotherapy (SLIT). Methods: Forty patients underwent IT with a birch extract (Staloral; Stallergenes, Antony, France), 20 by SCIT and 20 by SLIT. After 1 year of treatment, 15 patients (8 for SCIT and 7 for SLIT) accepted to undergo an oral apple challenge. Measurements of specific IgE to Bet v 1 and Mal d 1 and related allergens Api g 1 and Dau c 1 were obtained in 10 patients, at baseline and after IT. Results: Two of 8 SCIT-treated patients (25%) and 1 of 7 SLIT-treated patients (14.2%) developed complete tolerance to apple. In the remaining patients, an increase in the provocative dose was found in 3 of the SCIT-treated (37.5%) and 2 of the SLIT-treated patients (28.6%). Changes in the levels of specific IgE to Mal d 1 were unrelated to clinical results. Conclusions: These findings suggest that different doses of birch extract may be needed in different patients to improve the associated apple allergy and that a finer diagnostic work-up in selecting patients with birch-apple syndrome who are candidates to respond to birch pollen IT also concerning apple allergy is required.

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Section: Discussionmentioning

confidence: 99%

Birch-Apple Syndrome Treated with Birch Pollen Immunotherapy

Melato¹,

Russello²,

Incorvaia³

et al. 2011

Int Arch Allergy Immunol

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“…Non-specific lipid transfer proteins were purified from apple ( Malus domestica , Mal d 3), peach ( Prunus persica , Pru p 3) and hazelnut ( Corylus avellana , Cor a 8) as described previously [20]–[22]. 7S and 11S seed storage globulins were purified from hazelnut ( Corylus avellana , Cor a 11, Cor a 9) and peanut ( Arachis hypogaea , Ara h 1, Ara h 3) as described previously [22], [23].…”

Section: Methodsmentioning

confidence: 99%

High-Throughput NMR Assessment of the Tertiary Structure of Food Allergens

et al. 2012

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Background In vitro component-resolved diagnosis of food allergy requires purified allergens that have to meet high standards of quality. These include the authentication of their conformation, which is relevant for the recognition by specific IgE antibodies from allergic patients. Therefore, highly sensitive and reliable screening methods for the analysis of proteins/allergens are required to assess their structural integrity. In the present study one-dimensional 1H Nuclear Magnetic Resonance (1D 1H-NMR) analysis was adopted for the assessment of overall structural and dynamic properties and authentication of a set of relevant food allergens, including non-specific lipid transfer proteins from apple, peach and hazelnut, 7/8S seed storage globulins from hazelnut and peanut, 11S seed storage globulins from hazelnut and peanut, caseins from cows' and goats' milk and tropomyosin from shrimp.Methodology/Principal FindingsTwo sets of 1D 1H-NMR experiments, using 700 MHz and 600 MHz instruments at 298 K were carried out to determine the presence and the extent of tertiary structure. Structural similarity among members of the individual allergen families was also assessed and changes under thermal stress investigated. The nuclear magnetic resonance (NMR) results were compared with structural information available either from the literature, Protein Data Bank entries, or derived from molecular models.Conclusions/Significance1D 1H-NMR analysis of food allergens allowed their classification into molecules with rigid, extended and ordered tertiary structures, molecules without a rigid tertiary structure and molecules which displayed both features. Differences in thermal stability were also detected. In summary, 1D 1H-NMR gives insights into molecular fold of proteins and offers an independent method for assessing structural properties of proteins.

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“…Rosaceae fruits contain proteins homologous to the major birch pollen allergen Bet v 1, which are designated, Mal d 1, in apple and, Pru p 1, in peach. Both proteins were produced as recombinant proteins [37,38]. Also the nonspecific lipid transfer proteins are known as relevant allergens in fruits and both Mal d 3 and Pru p 3 were purified from fruit peel tissue [37,38].…”

Section: Allergens From the Europrevall Allergen Librarymentioning

confidence: 99%

Coordinated and standardized production, purification and characterization of natural and recombinant food allergens to establish a food allergen library

Hoffmann‐Sommergruber

Mills

Vieths

2008

Mol. Nutr. Food Res.

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Reliable diagnosis of food allergy is dependent on the analytes used. Approaches based on well-defined individual molecules of either natural or recombinant origin are likely to replace those based on food extracts in the future. Therefore, a library comprising well-characterized authentic natural and recombinant allergens was formed within the EC funded IP EuroPrevall. The advantages and disadvantages of including either natural or recombinant proteins are summarized, together with inclusion criteria such as purity and the implications of both allergenic and nonallergenic impurities for the performance of diagnostic assays. In order to harmonize quality criteria of the individual food allergens included in the library, as suite of characteristics and associated methodologies used to define them, was agreed. The application of these methods and impact on the quality and performance of the final purified food allergens included in the EuroPrevall allergen library is discussed.

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Purification and characterisation of relevant natural and recombinant apple allergens

Cited by 27 publications

References 44 publications

Birch-Apple Syndrome Treated with Birch Pollen Immunotherapy

Birch-Apple Syndrome Treated with Birch Pollen Immunotherapy

High-Throughput NMR Assessment of the Tertiary Structure of Food Allergens

Coordinated and standardized production, purification and characterization of natural and recombinant food allergens to establish a food allergen library

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