Natural and recombinant molecules of the cherry allergen Pru av 2 show diverse structural and B cell characteristics but similar T cell reactivity

Fuchs, H.; Bohle, Barbara; Dall’Antonia, Yuliya; Radauer, Christian; Hoffmann‐Sommergruber, Karin; Mari, Adriano; Scheiner, Otto; Keller, Walter; Breiteneder, Heimo

doi:10.1111/j.1365-2222.2006.02439.x

Cited by 32 publications

(18 citation statements)

References 36 publications

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“…Considering these associations, 16 TLPs were purified, from both foods and pollens, according to previously described methods (Table 1). Some of these food-related TLPs had been previously identified as allergens (www.allergen.org, IUIS; www.allergome.com): Act d 2 [8], Cup a 3 [21], Mal d 2 [22], Mus a 4 [23], Pru av 2 [24], Pru p 2.0101 [6], Pru p 2.0201 [6], a wheat TLP [25] and olive TLP [26]. The purified wheat TLP in this study proved to be different from the one associated with baker’s asthma.…”

Section: Resultsmentioning

confidence: 99%

The Involvement of Thaumatin-Like Proteins in Plant Food Cross-Reactivity: A Multicenter Study Using a Specific Protein Microarray

et al. 2012

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Cross-reactivity of plant foods is an important phenomenon in allergy, with geographical variations with respect to the number and prevalence of the allergens involved in this process, whose complexity requires detailed studies. We have addressed the role of thaumatin-like proteins (TLPs) in cross-reactivity between fruit and pollen allergies. A representative panel of 16 purified TLPs was printed onto an allergen microarray. The proteins selected belonged to the sources most frequently associated with peach allergy in representative regions of Spain. Sera from two groups of well characterized patients, one with allergy to Rosaceae fruit (FAG) and another against pollens but tolerant to food-plant allergens (PAG), were obtained from seven geographical areas with different environmental pollen profiles. Cross-reactivity between members of this family was demonstrated by inhibition assays. Only 6 out of 16 purified TLPs showed noticeable allergenic activity in the studied populations. Pru p 2.0201, the peach TLP (41%), chestnut TLP (24%) and plane pollen TLP (22%) proved to be allergens of probable relevance to fruit allergy, being mainly associated with pollen sensitization, and strongly linked to specific geographical areas such as Barcelona, Bilbao, the Canary Islands and Madrid. The patients exhibited >50% positive response to Pru p 2.0201 and to chestnut TLP in these specific areas. Therefore, their recognition patterns were associated with the geographical area, suggesting a role for pollen in the sensitization of these allergens. Finally, the co-sensitizations of patients considering pairs of TLP allergens were analyzed by using the co-sensitization graph associated with an allergen microarray immunoassay. Our data indicate that TLPs are significant allergens in plant food allergy and should be considered when diagnosing and treating pollen-food allergy.

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Section: Resultsmentioning

confidence: 99%

The Involvement of Thaumatin-Like Proteins in Plant Food Cross-Reactivity: A Multicenter Study Using a Specific Protein Microarray

et al. 2012

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“…Although this appears to be quite an unusual curve for a protein consisting mainly of β-sheet and β-turn structure, CD spectra of other TLPs (e.g. thaumatin [32, 33], zeamatin [34] and Pru av 2 [35]) suggest that this might be a common feature of this protein family [35]. After heating from 20 to 95°C at pH 7.0 the CD signal changed from one characteristic for a folded protein to one presenting a random coil.…”

Section: Resultsmentioning

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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“…Allergens of this group belonging to food allergens include Pru av 2 from cherries [125], Cap a 1 from bell pepper [62, 126], Mal d 2 from apple [127], Act d 2 from kiwi [128], and Pru p 2 from peach [129]. Pru av 2, the major allergen in cherries, is one of the main causes of oral allergy syndrome and shares considerable sequence identity with Jun a 3.…”

Section: Plant Pr Proteins and Allergenicitymentioning

confidence: 99%

Current Overview of Allergens of Plant Pathogenesis Related Protein Families

Sinha

Singh

Kushwaha

et al. 2014

The Scientific World Journal

183

109

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Pathogenesis related (PR) proteins are one of the major sources of plant derived allergens. These proteins are induced by the plants as a defense response system in stress conditions like microbial and insect infections, wounding, exposure to harsh chemicals, and atmospheric conditions. However, some plant tissues that are more exposed to environmental conditions like UV irradiation and insect or fungal attacks express these proteins constitutively. These proteins are mostly resistant to proteases and most of them show considerable stability at low pH. Many of these plant pathogenesis related proteins are found to act as food allergens, latex allergens, and pollen allergens. Proteins having similar amino acid sequences among the members of PR proteins may be responsible for cross-reactivity among allergens from diverse plants. This review analyzes the different pathogenesis related protein families that have been reported as allergens. Proteins of these families have been characterized in regard to their biological functions, amino acid sequence, and cross-reactivity. The three-dimensional structures of some of these allergens have also been evaluated to elucidate the antigenic determinants of these molecules and to explain the cross-reactivity among the various allergens.

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Natural and recombinant molecules of the cherry allergen Pru av 2 show diverse structural and B cell characteristics but similar T cell reactivity

Cited by 32 publications

References 36 publications

The Involvement of Thaumatin-Like Proteins in Plant Food Cross-Reactivity: A Multicenter Study Using a Specific Protein Microarray

The Involvement of Thaumatin-Like Proteins in Plant Food Cross-Reactivity: A Multicenter Study Using a Specific Protein Microarray

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

Current Overview of Allergens of Plant Pathogenesis Related Protein Families

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