Studies in food allergy

Tuft, Louis; Blumstein, George I.

doi:10.1016/s0021-8707(42)90070-4

Cited by 98 publications

(6 citation statements)

References 10 publications

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“…Structural similarity between two antigens can lead to cross-reactivity . This effect can also be observed when people being sensitized to pollen allergens develop an allergic reaction to certain fruits, due to related proteins in foods. , The similarity of the food allergen to the aeroallergen is based on either the amino acid (AA) sequence or their protein conformation . The latter is usually denatured during food processing due to, for example, heat, acids, and so on, and therefore, allergic reactions based on cross-allergy are primarily limited to fresh foods.…”

Section: Introductionmentioning

confidence: 99%

Characterization and Quantification of Mal d 1 Isoallergen Profiles and Contents in Traditional and Commercial Apple Varieties by Mass Spectrometry

Kaeswurm

Straub

Siegele³

et al. 2023

J. Agric. Food Chem.

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The apple allergy in Northern Europe is a cross-reaction to the birch pollen allergy. No correlation between the allergenicity of an apple variety and the content of the major apple allergen Mal d 1, a homologue to the Bet v 1 allergen in birch, could be found using ELISA, so far. Therefore, an impact of polyphenols and/or differences in the isoallergen profile are discussed. To allow a more detailed analysis of the Mal d 1 content and the isoallergen profile, a mass spectrometric method was applied to investigate differences in the flesh and peel of 10 traditional varieties and 10 commercial breeds. The data revealed often, but not always, lower Mal d 1 contents in traditional varieties grown in orchard meadows, which was more obvious in the flesh. Differences among the peels were less pronounced. A closer look at the individual isoallergens 1.01, 1.02, 1.03, and 1.06 reveals an increased impact of the minor isoallergens 1.03 and 1.06 on the allergenic potential, since commercial breeds like Braeburn, Santana, and Holstein Cox, which are considered to have reduced allergenic potentials, were characterized by low levels of these isoallergens.

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Section: Introductionmentioning

confidence: 99%

Characterization and Quantification of Mal d 1 Isoallergen Profiles and Contents in Traditional and Commercial Apple Varieties by Mass Spectrometry

Kaeswurm

Straub

Siegele³

et al. 2023

J. Agric. Food Chem.

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“…In addition, Mal d 1 also shares T cell epitopes with the major birch pollen allergen, Bet v 1 [10]. This homology is also reflected by the clinical observation that apple allergy starts after the onset of birch pollinosis [4,10,11,12]. The hypothesis suggests that Bet v 1 sensitization initiates allergic reactions to Mal d 1.…”

Section: Introductionmentioning

confidence: 99%

Mutational Analysis of Amino Acid Positions Crucial for IgE-Binding Epitopes of the Major Apple <i>(Malus domestica)</i> Allergen, Mal d 1

Gadermaier

Bohle

et al. 2005

Int Arch Allergy Immunol

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Background: Individual amino acid residues of the major birch pollen allergen, Bet v 1, have been identified to be crucial for IgE recognition. The objective of the present study was to evaluate whether this concept was applicable for the Bet v 1-homologous apple allergen, Mal d 1. Methods: A Mal d 1 five-point mutant was produced by PCR techniques, cloned into pMW 172 and expressed in Escherichia coli BL21(DE3) cells. To evaluate the allergenic properties of the engineered protein compared to Mal d 1 wild-type IgE immunoblotting, ELISA, peripheral blood monocytes proliferation assays, and skin prick tests were performed. Results: The Mal d 1 mutant showed reduced capacity to bind specific IgE as compared to wild-ype Mal d 1 in in vitro assays in the majority of the sera tested. In ELISA, 10 out of 14 serum samples displayed an 88–30% decrease in IgE binding to Mal d 1 mutant compared to wild-type Mal d 1. Skin prick tests in apple-allergic patients (n = 2) confirmed the markedly decreased ability of the Mal d 1 mutant to induce allergic reactions in vivo. However, the relevant T cell epitopes were present in the mutated molecule according to peripheral blood mononuclear cell proliferation assays. Conclusions: Our findings suggest that it is possible to modulate the IgE-binding properties of allergens by single amino acid substitutions at crucial positions which might be useful for future immunotherapy of birch-pollen-associated food allergies which are not ameliorated by birch pollen immunotherapy.

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“…Взаимосвязь между сезонной аллергией и пищевой гиперчувствительностью на растительные продукты впер-вые была отмечена L. Tuft и G. Blumstein в 1942 г. [8]. Однако термин ОАС был предложен намного позже -в 1987 г.…”

Section: Ige-опосредованная гастроинтестинальная пищевая аллергияunclassified

Gastrointestinal Food Allergy in Children

Макарова¹,

Намазова-Баранова²,

Вишнёва³

et al. 2017

Vopr. sovr. pediatr.

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ВВЕДЕНИЕРост распространенности пищевой аллергии, в том числе у детей, делает эту форму патологии все более актуальной проблемой педиатрии [1,2].Согласно определению, пищевая аллергия -это пато-логическая реакция на компоненты пищи, в основе которой лежат иммунные механизмы, включая выработку специфи-ческих иммуноглобулинов (Immunoglobulin, Ig) E (IgE-опо-сре дованные аллергические реакции), клеточный иммун-ный ответ (не-IgE-опосредованные аллергические реакции) и сочетание этих двух механизмов (реакции смешанного типа -IgE-опо средованные и не-IgE-опосредованные) [1]. При этом не-IgE-опосредованные аллергические реакции на пищу, особенно изолированные гастроинтестинальные проявления аллергии при отсутствии кожных высыпаний, вызывают наибольшие трудности в диагностике.Целью настоящего обзора является ознакомление педиатров с современными представлениями о патогенезе гастроинтестинальной пищевой аллергии и с актуальными принципами ее диагностики.

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Studies in food allergy

Cited by 98 publications

References 10 publications

Characterization and Quantification of Mal d 1 Isoallergen Profiles and Contents in Traditional and Commercial Apple Varieties by Mass Spectrometry

Characterization and Quantification of Mal d 1 Isoallergen Profiles and Contents in Traditional and Commercial Apple Varieties by Mass Spectrometry

Mutational Analysis of Amino Acid Positions Crucial for IgE-Binding Epitopes of the Major Apple <i>(Malus domestica)</i> Allergen, Mal d 1

Gastrointestinal Food Allergy in Children

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