Digested Ara h 1 has sensitizing capacity in Brown Norway rats

Bøgh, Katrine Lindholm; Kroghsbo, Stine; Dahl, L.; Rigby, Neil M.; Barkholt, Vibeke; Mills, E. N. Clare; Madsen, Charlotte Bernhard

doi:10.1111/j.1365-2222.2009.03333.x

Cited by 57 publications

(82 citation statements)

References 49 publications

(76 reference statements)

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“…Gastric digestion was performed essentially as described by Bøgh et al 10 In short, pepsin immobilized to agarose (P0609, Sigma, St. Louis, MO) was washed two times (100g, 1 min) in 10 mL of 1 mM HCl. Purified Ara h 1 (2.4 mg/mL in 150 mM NaCl) was adjusted to pH 2.5 with 1 M HCl and added to the immobilized pepsin to yield an activity of pepsin of approximately 170 U per mg Ara h 1.…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

“…23,24 Ara h 1 is a readily digestible allergen, being digested to small peptide fragments by gastroduodenal digestion. 9,10 Even though Ara h 1 is a labile protein, Eiwegger et al 9 and Bøgh et al 10 showed that the digestion products of Ara h 1 retain allergenic potential, being able to sensitize as well as elicit allergic reactions. These studies indicated that aggregation of peptides may play a major role in maintaining allergenic activity.…”

Section: ■ Introductionmentioning

confidence: 99%

“…We have previously shown that peptide fragments, as small as 2 kDa, have the capacity to sensitize and elicit allergic reactions. 10 In the present study, we focus on examining under which conditions such peptide fragments retain their allergenic potential.…”

Section: ■ Introductionmentioning

confidence: 99%

“…11−13 However, while pepsin stability as a part of an allergenicity assessment would still seem reasonable for the purpose of safety evaluation of most food proteins, we now know that for some allergenic proteins, this approach would be misleading. The milk allergen β-casein (Bos d 8) 7,14,15 as well as the peanut allergen Ara h 1 9,10 have several times been shown to be easily digestible food allergens.…”

Section: ■ Introductionmentioning

confidence: 99%

“…Epitope mapping studies of this protein have suggested both linear 21 and conformational 25 IgEbinding epitopes, at least some of which are able to survive the digestion process. 10,26 Peptides need to have a certain size to be allergenic, but the exact lower molecular weight (MW) size limit is not known. Yet, many suggestions for such a lower MW size limit have been presented, 11,27−31 and the general view appears to be that peptides need to be approximately 3.5 kDa to contain sensitizing and eliciting allergenic capacity.…”

Section: ■ Introductionmentioning

confidence: 99%

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Digested Ara h 1 Loses Sensitizing Capacity When Separated into Fractions

Bøgh

Barkholt²,

Rigby

et al. 2012

J. Agric. Food Chem.

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The major peanut allergen Ara h 1 is an easily digestible protein under physiological conditions. The present study revealed that pepsin digestion products of Ara h 1 retained the sensitizing potential in a Brown Norway rat model, while this sensitizing capacity was lost by separating the digest into fractions by gel permeation chromatography. Protein chemical analysis showed that the peptide composition as well as the aggregation profiles of the fractions of Ara h 1 digest differed from that of the whole pool. These results indicate that the sensitizing capacity of digested Ara h 1 is a consequence of the peptides being in an aggregated state resembling the intact molecule or that most peptides of the digests need to be present in the same solution, having a synergistic or adjuvant effect and thereby augmenting the immune response against other peptides.

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Section: ■ Materials and Methodsmentioning

confidence: 99%

Section: ■ Introductionmentioning

confidence: 99%

Section: ■ Introductionmentioning

confidence: 99%

Section: ■ Introductionmentioning

confidence: 99%

Section: ■ Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Digested Ara h 1 Loses Sensitizing Capacity When Separated into Fractions

Bøgh

Barkholt²,

Rigby

et al. 2012

J. Agric. Food Chem.

View full text Add to dashboard Cite

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Animal Models for the Study of Food Allergies

2023

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In the last decades there has been a parallel increase in the incidence of food allergies and the development of experimental mouse models. These models have improved our understanding of the disease but do have limitations. For instance, they do not entirely reproduce human pathophysiology; moreover, validated and predictive models are absent. Nevertheless, the models provide opportunities to further understand fundamental disease mechanisms. The selection of any of the many experimental models depends on the research aims. This overview focuses on IgE-mediated food allergy in wild-type, genetically modified, and humanized mouse models and presents a comprehensive overview of the currently used protocols, challenges, and limitations, as well as provides guidelines for model selection based on the three critical areas of research: 1) safety assessment, 2) evaluating treatment, and 3) elucidating pathophysiology.

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