Genomic characterization and linkage mapping of the apple allergen genes Mal d 2 (thaumatin-like protein) and Mal d 4 (profilin)

Gao, Zhongshan; Weg, Eric van de; Schaart, Jan G.; Arkel, Gert van; Breiteneder, Heimo; Hoffmann‐Sommergruber, Karin; Gilissen, L.J.W.J.

doi:10.1007/s00122-005-0034-z

Cited by 51 publications

(42 citation statements)

References 31 publications

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“…To date, four apple allergens have been identified: the Bet v 1 homologue Mal d 1 [1], the thaumatin-like protein (TLP) Mal d 2 [2], the nonspecific lipid transfer protein (nsLTP) Mal d 3 [3], and the apple profilin Mal d 4 [2]. While in Northern and Central Europe the occurrence of allergy to apple is frequently related to birch pollinosis and sensitization is due to cross-reactivity between Bet v 1 and Mal d 1, in Southern Europe this fruit allergy is observed together with allergy to peach caused by the allergens Pru p 3 and Mal d 3 [4].…”

Section: Introductionmentioning

confidence: 99%

Mal d 2, the Thaumatin-Like Allergen from Apple, Is Highly Resistant to Gastrointestinal Digestion and Thermal Processing

Smole

Bublin

Radauer

et al. 2008

Int Arch Allergy Immunol

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Background: The stability of food allergens to proteolysis and thermal denaturation contributes considerably to their allergenicity. Methods: Mal d 2, an allergenic thaumatin-like protein (TLP) from apple, was isolated and purified by anion exchange chromatography. Its IgE reactivity was tested by ELISA and immunoblotting using sera from apple allergic patients. The proteolytic stability of Mal d 2 was investigated using two in vitro digestion models. Effects of thermal treatment at different pH values on the secondary structure of the protein were recorded by circular dichroism. The level and IgE reactivity of Mal d 2 present in industrially prepared foods were assessed. Results: Purified Mal d 2 consisted of two isoforms. Both harbored carbohydrate moieties and bound serum IgE from apple allergic individuals. Mal d 2 showed remarkable stability to proteolysis and thermal treatments. The allergen remained intact after 2 h each of gastric and subsequent duodenal digestion retaining its full IgE-binding capacity. Mal d 2 was unfolded at neutral and acidic pH at 70°C. Refolding after cooling was only observed at acidic pH. Mal d 2 detected by an anti-TLP antibody in cloudy apple juice did not bind IgE of a serum pool of apple allergic patients. Conclusion: Our findings suggest that Mal d 2 maintains its structure in the gastrointestinal tract, a feature essential for sensitizing the mucosal immune system and provoking allergic reactions.

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Section: Introductionmentioning

confidence: 99%

Mal d 2, the Thaumatin-Like Allergen from Apple, Is Highly Resistant to Gastrointestinal Digestion and Thermal Processing

Smole

Bublin

Radauer

et al. 2008

Int Arch Allergy Immunol

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“…The Act d 2 sequence obtained from the gDNA of green kiwifruit encoded a 201 amino acid protein. Unlike Mal d 2 [34], no intron was found in the genomic sequence of Act d 2. As shown for the plant expressed rMal d 2 [35], mature Act d 2 does not seem to be glycosylated.…”

Section: Discussionmentioning

confidence: 57%

Quantification of the thaumatin‐like kiwi allergen by a monoclonal antibody‐based ELISA

Gavrović-Jankulović¹,

Spasic

Veličković

et al. 2008

Molecular Nutrition Food Res

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Thaumatin-like proteins (TLPs) have been established as a new family of fruit and pollen allergens. The aim of this study was to develop a two-site ELISA for the quantification of the thaumatin-like kiwi allergen (Act d 2) in kiwifruit extracts and kiwifruit-containing food products. Genomic DNA (gDNA) of Act d 2 was amplified and the deduced amino acid sequence was determined to obtain a primary structure. Act d 2 purified from kiwifruit extract by HPLC was identified by Edman degradation and MS. Balb/c mice were immunized with Act d 2 for the production of mAbs by hybridoma technology. The optimized ELISA measured Act d 2 concentrations ranging from 0.2 to 9.0 ng/mL, with intra- and interassay coefficients of variation of 3.65 and 10.44%, respectively. The developed ELISA is a useful method for the quantification of the thaumatin-like kiwi allergen in kiwifruit extracts as well as the allergen level in kiwifruit-containing food products. It may be a helpful analytical tool for the evaluation of the stability (integrity) of fruit allergen extracts for in vitro diagnosis.

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“…It has been reported different degrees of polymorphism in diverse allergen sources, which include dust mites (Piboonpocanun et al 2006), food (Hales et al 2004, Gao et al 2005 and pollen allergens of different tree species and herbaceous (Chang et al 1999). However, although the polymorphism is beginning to be detailed in depth, relatively little is known about the causes which originate.…”

Section: Molecular Characteristics Of Profilin Explain the Pan-allergmentioning

confidence: 99%

“…In other allergens, the presence of multiple forms of the allergen can be explained by the existence of posttranslational modifications (Batanero et al 1996a). In apple (Malus domestica), have been characterized up to 18 genes of Mal d 1, and there is differences in allergenicity depending on the cultivar (Gao et al 2005) which may be due to this extensive allelic diversity. In olive, it has been shown that polymorphism of the allergen Ole e 1 is clearly linked to genetic background (cultivar) (Hamman-Khalifa et al 2008), similarly to what happens to Ole e 2, where there are differential molecular characteristics due to polymorphism, which would be sufficient to explain the differences in reactivity allergenic / immunogenic among profilins from different species, different olive varieties, and even among the same isoforms of profilins (JimenezLopez 2008;Jimenez-Lopez et al 2012).…”

Section: Molecular Characteristics Of Profilin Explain the Pan-allergmentioning

confidence: 99%

Differential Immune-Reactivity and Subcellular Distribution Reveal the Multifunctional Character of Profilin in Pollen as Major Effect of Sequences Polymorphism

Jiménez-López¹,

Morales²,

Volkmann³

et al. 2012

Current Insights in Pollen Allergens

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Genomic characterization and linkage mapping of the apple allergen genes Mal d 2 (thaumatin-like protein) and Mal d 4 (profilin)

Cited by 51 publications

References 31 publications

Mal d 2, the Thaumatin-Like Allergen from Apple, Is Highly Resistant to Gastrointestinal Digestion and Thermal Processing

Mal d 2, the Thaumatin-Like Allergen from Apple, Is Highly Resistant to Gastrointestinal Digestion and Thermal Processing

Quantification of the thaumatin‐like kiwi allergen by a monoclonal antibody‐based ELISA

Differential Immune-Reactivity and Subcellular Distribution Reveal the Multifunctional Character of Profilin in Pollen as Major Effect of Sequences Polymorphism

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