Assessment of Allergenic Activity of a Heat-Coagulated Ovalbumin after<i>in Vivo</i>Digestion

Joo, Kana; Kato, Yasuko

doi:10.1271/bbb.70.591

Cited by 32 publications

(25 citation statements)

References 17 publications

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“…7,[9][10][11] Although ovalbumin is the most abundant protein found in egg white, it is sensitive to thermal denaturation, with a resultant decrease in allergenicity. 12 In contrast, ovomucoid is heat resistant and remains soluble after extensive heating. Deutsch and Morton 13 found that purified ovomucoid heated for 1 hour at 1008C retained its antibody-binding activity.…”

mentioning

confidence: 99%

Immunologic changes in children with egg allergy ingesting extensively heated egg

Lemon-Mulé

Sampson

Sicherer

et al. 2008

Journal of Allergy and Clinical Immunology

430

425

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mentioning

confidence: 99%

Immunologic changes in children with egg allergy ingesting extensively heated egg

Lemon-Mulé

Sampson

Sicherer

et al. 2008

Journal of Allergy and Clinical Immunology

430

425

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“…During systemic anaphylaxis, decreases in both whole body temperature and rates of voluntary physical activity are commonly observed [29,30,31]. An oral dose of 0.1 mg of ω-5 gliadin was administered in this experiment.…”

Section: Resultsmentioning

confidence: 99%

Exercise-Independent Wheat-Induced Anaphylaxis Caused by ω-5 Gliadin in Mice

Tanaka

Nagano²,

Yano³

et al. 2011

Int Arch Allergy Immunol

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Background: ω-5 Gliadin is known as a major allergen in wheat-dependent exercise-induced anaphylaxis. The characteristics that make ω-5 gliadin an allergen remain unclear. Methods: Mice were sensitized by means of intraperitoneal injection of gliadin fractions together with the adjuvant alum. Anaphylactic responses were assessed by measuring body temperature and voluntary physical activity. Specific IgE levels in mouse serum were evaluated by ELISA. After oral administration of proteins to mice, concentrations of administered proteins in their portal blood were also analyzed by competitive inhibition ELISA. Results: Oral administration of ω-5 gliadin evoked significant decreases in body temperature and physical activity of sensitized mice, whereas the gliadin fraction did not induce these effects at the same dose. These responses were exercise independent. ELISA analysis revealed that IgE antibodies from sensitized mice react to ω-5 gliadin with great efficacy. After oral administration of either the gliadin fraction or ω-5 gliadin, blood levels of ω-5 gliadin were much higher than those of the gliadin fraction. Conclusions: ω-5 Gliadin caused anaphylaxis in sensitized mice, whereas the gliadin fraction did not at the same dose. The anaphylactic response was exercise independent. It is likely that IgE of sensitized mice reacts strongly to ω-5 gliadin and that ω-5 gliadin is better absorbed from the gastrointestinal tract than other components of the gliadin fraction. These results indicated that ω-5 gliadin has prominent characteristics as an allergen and that exercise might be an indirect factor in anaphylaxis induction.

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“…This is largely because of heat-labile epitopes of ovalbumin, which demonstrate significantly reduced IgE binding after heat denaturation [16]. By contrast, ovomucoid is able to retain its antibody-binding activity, even after extensive heating [9,[17][18][19].…”

Section: Egg Allergensmentioning

confidence: 99%