Increased allergen production in turnip (Brassica rapa) by treatments activating defense mechanisms☆☆☆★

Hänninen, Anna-Riitta; Mikkola, Janne; Kalkkinen, Nisse; Turjanmaa, Kristiina; Ylitalo, Leea; Reunala, Timo; Palosuo, Timo

doi:10.1016/s0091-6749(99)70135-1

Cited by 60 publications

(23 citation statements)

References 37 publications

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“…Native AMP Is Not Recognized by Hevein-specific IgE-To study the immunological properties of AMP, it was extracted from amaranth seeds and purified by affinity chromatography on a chitin column and reversed-phase HPLC as described previously for hevein (24). The molecular mass (3184.8 Da) of the purified protein corresponded to that calculated from the AMP sequence with three disulfide bonds (3183.7 Da).…”

Section: Hevein and Thementioning

confidence: 99%

The Major Conformational IgE-binding Epitopes of Hevein (Hev b6.02) Are Identified by a Novel Chimera-based Allergen Epitope Mapping Strategy

Karisola¹,

Alenius²,

Mikkola³

et al. 2002

Journal of Biological Chemistry

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A novel approach to localize and reconstruct conformational IgE-binding epitope regions of hevein (Hev b6.02), a major natural rubber latex allergen, is described. An antimicrobial protein (AMP) from the amaranth Amaranthus caudatus was used as an immunologically non-IgE-binding adaptor molecule to which terminal or central parts of hevein were fused. Hevein and AMP share a structurally identical core region but have different N-terminal and C-terminal regions. Only 1 of 16 hevein-allergic patients showed weak IgE binding to purified native or recombinant AMP. Chimeric AMP with the hevein N terminus was recognized by IgE from 14 (88%) patients, and chimeric AMP with the hevein C terminus was recognized by IgE from 6 (38%) patients. In contrast, chimeric AMP containing the hevein core region was recognized by IgE from only two patients. When both the N-terminal and C-terminal regions of hevein were fused with the AMP core, IgE from all 16 patients bound to the chimera. This chimera was also able to significantly inhibit (>70%) IgE binding to the native hevein. On the contrary, linear synthetic peptides corresponding to hevein regions in the AMP chimeras showed no significant IgE binding capacity in either enzyme-linked immunosorbent assay or inhibition enzyme-linked immunosorbent assay. These results suggest that the IgE binding ability of hevein is essentially determined by its N-terminal and C-terminal regions and that major IgE-binding epitopes of hevein are conformational. The chimera-based epitope mapping strategy described here provides a valuable tool for defining structural epitopes and creating specific reagents for allergen immunotherapy.

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Section: Hevein and Thementioning

confidence: 99%

The Major Conformational IgE-binding Epitopes of Hevein (Hev b6.02) Are Identified by a Novel Chimera-based Allergen Epitope Mapping Strategy

Karisola¹,

Alenius²,

Mikkola³

et al. 2002

Journal of Biological Chemistry

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“…The sequence of the induced turnip allergen was similar to those of prohevein (Hev b 6.01) and proteins belonging to the PR-4 family. The authors of this study concluded that activating the defense mechanisms of plants may considerably increase their allergen content (Hänninen et al, 1999). There is also a potential for the induction of cross-reactive plant allergens by environmental pollutants (Masuch et al, 1997;Midoro-Horiuti et al, 2000, 2001.…”

Section: Induction Of Cross-reactive Plant Allergensmentioning

confidence: 86%

“…A cross-reactive endochitinase in avocado (Pers a 1) was actually induced by infectious pathogen and ethylene treatments (Sánchez-Monge et al, 2000). Similarly, a cross-reactive allergen in a turnip was increased up to 10 times by treating the plant with salicylic acid or ethephon (Hänninen et al, 1999). The sequence of the induced turnip allergen was similar to those of prohevein (Hev b 6.01) and proteins belonging to the PR-4 family.…”

Section: Induction Of Cross-reactive Plant Allergensmentioning

confidence: 91%

Features and Mode of Action of Cross-reactive Plant Allergens Relevant to Latex-fruit Syndrome

Yagami

2002

Food and Agricultural Immunology

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Immediate-type reactions to articles made from natural rubber latex are collectively referred to as latex allergy. Some latex-sensitized patients also experience allergic reactions to various fruits and vegetables. This phenomenon is RESEARCH ON ALLERGENSThere have been recent surprising advancements in immunology, and we expect it to progress even more rapidly and steadily in the future using the genomic information of the human being. By contrast, research on allergenic substances (allergens) is far behind the times. The accumulation of scientific knowledge about the features and modes of action of allergens is

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“…As the hevein domain comprises most of the molecule's allergenicity, two more allergens should be mentioned although displaying no chitinase activity, i.e. Bra r 2 (turnip rape) with a prohevein-like domain composition [42] and the wheat germ agglutinin Tri a 18, a lectin, consisting of four hevein-like domains. In summary, most of the allergenic activity of chitinases seems to be due to the hevein-like domain.…”

Section: Pr-3 Family or Class I Chitinasesmentioning

confidence: 99%

Molecular Properties of Plant Food Allergens: A Current Classification into Protein Families

Hauser¹,

Egger²,

Wallner³

et al. 2008

TOIJ

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So far the allergen list of the International Union of Immunological Societies (IUIS) allergen nomenclature subcommittee comprises 130 plant-derived food allergens. Based on sequence homology these allergens can be classified into only 27 out of 9,000 known protein families according to the Allfam database. These families comprise the prolamin and cupin superfamilies, pathogenesis related proteins, profilins, thaumatin-like proteins, oleosins, expansins, a number of enzymes and protease inhibitors among others. The classification on structural and thus biochemical and functional similarities will provide a new outlook on the molecules and might contribute to answer the question about allergenicity of different proteins. This will help to define clinical relevant allergenic molecules and explain cross-reactive phenomena between single food allergen sources as well as between food allergens and allergenic molecules of other origins (e.g. pollen).

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Increased allergen production in turnip (Brassica rapa) by treatments activating defense mechanisms☆☆☆★

Cited by 60 publications

References 37 publications

The Major Conformational IgE-binding Epitopes of Hevein (Hev b6.02) Are Identified by a Novel Chimera-based Allergen Epitope Mapping Strategy

The Major Conformational IgE-binding Epitopes of Hevein (Hev b6.02) Are Identified by a Novel Chimera-based Allergen Epitope Mapping Strategy

Features and Mode of Action of Cross-reactive Plant Allergens Relevant to Latex-fruit Syndrome

Molecular Properties of Plant Food Allergens: A Current Classification into Protein Families

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