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Characterization of the allergenic potential of proteins: an assessment of the kiwifruit allergen actinidin.
J Appl Toxicol 2014; 34(5):489-97JA

Abstract

Assessment of the potential allergenicity (IgE-inducing properties) of novel proteins is an important challenge in the overall safety assessment of foods. Resistance to digestion with pepsin is commonly measured to characterize allergenicity, although the association is not absolute. We have previously shown that specific IgE antibody production induced by systemic [intraperitoneal (i.p.)] exposure of BALB/c strain mice to a range of proteins correlates with allergenic potential for known allergens. The purpose of the present study was to explore further the utility of these approaches using the food allergen, actinidin. Recently, kiwifruit has become an important allergenic foodstuff, coincident with its increased consumption, particularly as a weaning food. The ability of the kiwifruit allergen actinidin to stimulate antibody responses has been compared with the reference allergen ovalbumin, and with the non-allergen bovine haemoglobin. Haemoglobin was rapidly digested by pepsin whereas actinidin was resistant unless subjected to prior chemical reduction (reflecting intracellular digestion conditions). Haemoglobin stimulated detectable IgG antibody production at relatively high doses (10%), but failed to provoke detectable IgE. In contrast, actinidin was both immunogenic and allergenic at relatively low doses (0.25% to 1%). Vigorous IgG and IgG1 antibody and high titre IgE antibody responses were recorded, similar to those provoked by ovalbumin. Thus, actinidin displays a marked ability to provoke IgE, consistent with allergenic potential. These data provide further encouragement that in tandem with analysis of pepsin stability, the induction of IgE after systemic exposure of BALB/c strain mice provides a useful approach for the prospective identification of protein allergens.

Authors+Show Affiliations

Faculty of Life Sciences, The University of Manchester, Michael Smith Building, Oxford Road, Manchester, M13 9PT, UK.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

23754484

Citation

Dearman, Rebecca J., et al. "Characterization of the Allergenic Potential of Proteins: an Assessment of the Kiwifruit Allergen Actinidin." Journal of Applied Toxicology : JAT, vol. 34, no. 5, 2014, pp. 489-97.
Dearman RJ, Beresford L, Foster ES, et al. Characterization of the allergenic potential of proteins: an assessment of the kiwifruit allergen actinidin. J Appl Toxicol. 2014;34(5):489-97.
Dearman, R. J., Beresford, L., Foster, E. S., McClain, S., & Kimber, I. (2014). Characterization of the allergenic potential of proteins: an assessment of the kiwifruit allergen actinidin. Journal of Applied Toxicology : JAT, 34(5), pp. 489-97. doi:10.1002/jat.2897.
Dearman RJ, et al. Characterization of the Allergenic Potential of Proteins: an Assessment of the Kiwifruit Allergen Actinidin. J Appl Toxicol. 2014;34(5):489-97. PubMed PMID: 23754484.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Characterization of the allergenic potential of proteins: an assessment of the kiwifruit allergen actinidin. AU - Dearman,Rebecca J, AU - Beresford,Lorna, AU - Foster,Emily S, AU - McClain,Scott, AU - Kimber,Ian, Y1 - 2013/06/10/ PY - 2013/03/07/received PY - 2013/04/18/revised PY - 2013/04/18/accepted PY - 2013/6/12/entrez PY - 2013/6/12/pubmed PY - 2014/11/18/medline KW - IgE KW - allergenicity KW - animal models KW - genetically modified KW - kiwi fruit SP - 489 EP - 97 JF - Journal of applied toxicology : JAT JO - J Appl Toxicol VL - 34 IS - 5 N2 - Assessment of the potential allergenicity (IgE-inducing properties) of novel proteins is an important challenge in the overall safety assessment of foods. Resistance to digestion with pepsin is commonly measured to characterize allergenicity, although the association is not absolute. We have previously shown that specific IgE antibody production induced by systemic [intraperitoneal (i.p.)] exposure of BALB/c strain mice to a range of proteins correlates with allergenic potential for known allergens. The purpose of the present study was to explore further the utility of these approaches using the food allergen, actinidin. Recently, kiwifruit has become an important allergenic foodstuff, coincident with its increased consumption, particularly as a weaning food. The ability of the kiwifruit allergen actinidin to stimulate antibody responses has been compared with the reference allergen ovalbumin, and with the non-allergen bovine haemoglobin. Haemoglobin was rapidly digested by pepsin whereas actinidin was resistant unless subjected to prior chemical reduction (reflecting intracellular digestion conditions). Haemoglobin stimulated detectable IgG antibody production at relatively high doses (10%), but failed to provoke detectable IgE. In contrast, actinidin was both immunogenic and allergenic at relatively low doses (0.25% to 1%). Vigorous IgG and IgG1 antibody and high titre IgE antibody responses were recorded, similar to those provoked by ovalbumin. Thus, actinidin displays a marked ability to provoke IgE, consistent with allergenic potential. These data provide further encouragement that in tandem with analysis of pepsin stability, the induction of IgE after systemic exposure of BALB/c strain mice provides a useful approach for the prospective identification of protein allergens. SN - 1099-1263 UR - https://www.unboundmedicine.com/medline/citation/23754484/Characterization_of_the_allergenic_potential_of_proteins:_an_assessment_of_the_kiwifruit_allergen_actinidin_ L2 - https://doi.org/10.1002/jat.2897 DB - PRIME DP - Unbound Medicine ER -