Digestibility of allergens extracted from natural rubber latex and vegetable foods

Yagami, Takeshi; Haishima, Yuji; Nakamura, Akitada; Osuna, Hiroyuki; Ikezawa, Zenrō

doi:10.1067/mai.2000.109171

Cited by 102 publications

(85 citation statements)

References 40 publications

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“…Since 1996 a few individuals have questioned the relevance or predictive value of assessing the stability of the introduced protein to pepsin at low pH, or the conditions of the assay [49, 92, 93]. Clearly the pepsin assay is not 100% predictive, but many important food allergens are stable in pepsin at pH 1.2, suggesting the assay may be useful in risk assessment [39, 40].…”

Section: Protein Stability To Pepsinmentioning

confidence: 99%

Assessing Genetically Modified Crops to Minimize the Risk of Increased Food Allergy: A Review

Goodman

Hefle

Taylor

et al. 2005

Int Arch Allergy Immunol

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The first genetically modified (GM) crops approved for food use (tomato and soybean) were evaluated for safety by the United States Food and Drug Administration prior to commercial production. Among other factors, those products and all additional GM crops that have been grown commercially have been evaluated for potential increases in allergenic properties using methods that are consistent with the current understanding of food allergens and knowledge regarding the prediction of allergenic activity. Although there have been refinements, the key aspects of the evaluation have not changed. The allergenic properties of the gene donor and the host (recipient) organisms are considered in determining the appropriate testing strategy. The amino acid sequence of the encoded protein is compared to all known allergens to determine whether the protein is a known allergen or is sufficiently similar to any known allergen to indicate an increased probability of allergic cross-reactivity. Stability of the protein in the presence of acid with the stomach protease pepsin is tested as a risk factor for food allergenicity. In vitro or in vivo human IgE binding are tested when appropriate, if the gene donor is an allergen or the sequence of the protein is similar to an allergen. Serum donors and skin test subjects are selected based on their proven allergic responses to the gene donor or to material containing the allergen that was matched in sequence. While some scientists and regulators have suggested using animal models, performing broadly targeted serum IgE testing or extensive pre- or post-market clinical tests, current evidence does not support these tests as being predictive or practical. Based on the evidence to date, the current assessment process has worked well to prevent the unintended introduction of allergens in commercial GM crops.

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Section: Protein Stability To Pepsinmentioning

confidence: 99%

Assessing Genetically Modified Crops to Minimize the Risk of Increased Food Allergy: A Review

Goodman

Hefle

Taylor

et al. 2005

Int Arch Allergy Immunol

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“…An allergen's stability in the highly denaturing conditions of the stomach has important consequences in the maintenance of its antigenic epitopes and its allergenic potential [15,16]. However, few studies have been published on the structural characterization of these allergens under acidic conditions.…”

Section: Introductionmentioning

confidence: 99%

Stability of the allergenic soybean Kunitz trypsin inhibitor

Roychaudhuri

Sarath

Zeece

et al. 2004

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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The soybean Kunitz trypsin inhibitor (SKTI) is a 21.5 kDa allergenic protein that belongs to the family of all antiparallel h-sheet proteins that are highly resistant to thermal and chemical denaturation. Spectroscopic and biochemical techniques such as circular dichroism (CD), ANS fluorescence and proteolysis were used to study its molecular structure under denaturing conditions such as acid and heat to which these allergens are commonly exposed during food processing. Reduction of native SKTI leads to its complete and rapid proteolysis by pepsin in simulated gastric fluid (SGF). Limited proteolysis with chymotrypsin during renaturation after heating showed that the native structure reforms at around 60 jC reversing the denaturation. CD spectra revealed that under acid denaturing conditions, SKTI shows major changes in conformation, indicating the possibility of a molten structure. The existence of this intermediate was established by ANS fluorescence studies at different concentrations of HCl. The remarkable stability of SKTI to both thermal and acid denaturation may be important for its role as a food allergen. D

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“…One approach, therefore, is to characterize the susceptibility of the protein of interest to digestion by pepsin or in a simulated gastric fluid. However, this approach alone may not be sufficient to identify cross-reactive proteins with the potential to elicit allergic responses in food-or latex-sensitized individuals as in the case of oral allergy syndrome or latex-fruit syndrome (Yagami et al, 2000). Nor are considerations of stability to digestion necessarily relevant for allergens that act through dermal or inhalation exposure and that may have significance for worker health.…”

Section: Production Of Toxinsmentioning

confidence: 99%