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Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy.
Food Chem Toxicol 2012; 50(3-4):1013-8FC

Abstract

Actinidin, an abundant cysteine protease from kiwifruit, is a specific biomarker of isolated allergy to kiwifruit. This study evaluates the IgE-binding properties of biologically active and thermally inactivated actinidin. Employing two different activity assays (caseinolytic assay and zymogram with gelatin) we showed that actinidin obtained from kiwifruit extract under native conditions represents a mixture of inactive and active enzyme. The structural integrity of actinidin was confirmed by SDS-PAGE, Edman degradation, mass fingerprint and Western blot with polyclonal antibodies. Although it was capable of inducing positive skin prick test reactions, we failed to detect IgE reactivity of active actinidin in Western blot with patient sera. Thermally inactivated actinidin exhibited IgE reactivity both in vivo and in vitro, indicating that heat processed kiwifruit products may induce clinical reactivity. These findings imply that apart from the allergenic epitopes on its surface, actinidin also contains hidden epitopes inside the protein which become accessible to IgE upon thermal treatment.

Authors+Show Affiliations

Department of Biochemistry, Faculty of Chemistry, University of Belgrade, and Department of Allergology and Pulmonology, University Children's Hospital, Belgrade 11000, Serbia.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo 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

22227218

Citation

Grozdanovic, Milica, et al. "Evaluation of IgE Reactivity of Active and Thermally Inactivated Actinidin, a Biomarker of Kiwifruit Allergy." Food and Chemical Toxicology : an International Journal Published for the British Industrial Biological Research Association, vol. 50, no. 3-4, 2012, pp. 1013-8.
Grozdanovic M, Popovic M, Polovic N, et al. Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy. Food Chem Toxicol. 2012;50(3-4):1013-8.
Grozdanovic, M., Popovic, M., Polovic, N., Burazer, L., Vuckovic, O., Atanaskovic-Markovic, M., ... Gavrovic-Jankulovic, M. (2012). Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy. Food and Chemical Toxicology : an International Journal Published for the British Industrial Biological Research Association, 50(3-4), pp. 1013-8. doi:10.1016/j.fct.2011.12.030.
Grozdanovic M, et al. Evaluation of IgE Reactivity of Active and Thermally Inactivated Actinidin, a Biomarker of Kiwifruit Allergy. Food Chem Toxicol. 2012;50(3-4):1013-8. PubMed PMID: 22227218.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy. AU - Grozdanovic,Milica, AU - Popovic,Milica, AU - Polovic,Natalija, AU - Burazer,Lidija, AU - Vuckovic,Olga, AU - Atanaskovic-Markovic,Marina, AU - Lindner,Buko, AU - Petersen,Arnd, AU - Gavrovic-Jankulovic,Marija, Y1 - 2011/12/28/ PY - 2011/10/31/received PY - 2011/12/13/revised PY - 2011/12/19/accepted PY - 2012/1/10/entrez PY - 2012/1/10/pubmed PY - 2012/7/17/medline SP - 1013 EP - 8 JF - Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association JO - Food Chem. Toxicol. VL - 50 IS - 3-4 N2 - Actinidin, an abundant cysteine protease from kiwifruit, is a specific biomarker of isolated allergy to kiwifruit. This study evaluates the IgE-binding properties of biologically active and thermally inactivated actinidin. Employing two different activity assays (caseinolytic assay and zymogram with gelatin) we showed that actinidin obtained from kiwifruit extract under native conditions represents a mixture of inactive and active enzyme. The structural integrity of actinidin was confirmed by SDS-PAGE, Edman degradation, mass fingerprint and Western blot with polyclonal antibodies. Although it was capable of inducing positive skin prick test reactions, we failed to detect IgE reactivity of active actinidin in Western blot with patient sera. Thermally inactivated actinidin exhibited IgE reactivity both in vivo and in vitro, indicating that heat processed kiwifruit products may induce clinical reactivity. These findings imply that apart from the allergenic epitopes on its surface, actinidin also contains hidden epitopes inside the protein which become accessible to IgE upon thermal treatment. SN - 1873-6351 UR - https://www.unboundmedicine.com/medline/citation/22227218/Evaluation_of_IgE_reactivity_of_active_and_thermally_inactivated_actinidin_a_biomarker_of_kiwifruit_allergy_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0278-6915(11)00696-X DB - PRIME DP - Unbound Medicine ER -