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Isolation and biochemical characterization of a thaumatin-like kiwi allergen
dc.creator | Gavrović-Jankulović, Marija | |
dc.creator | Ćirković, Tanja | |
dc.creator | Vučković, Olga | |
dc.creator | Atanasković-Marković, Marina | |
dc.creator | Petersen, Arnd | |
dc.creator | Gojgić, G. | |
dc.creator | Burazer, Lidija | |
dc.creator | Jankov, Ratko | |
dc.date.accessioned | 2021-02-18T10:24:50Z | |
dc.date.available | 2021-02-18T10:24:50Z | |
dc.date.issued | 2002 | |
dc.identifier.issn | 0091-6749 | |
dc.identifier.uri | http://intor.torlakinstitut.com/handle/123456789/150 | |
dc.description.abstract | Background: Kiwi fruit allergy, as well as its association with hypersensitivity to other foods and to pollen, has been extensively reported in the last few years. Several IgE-binding components have been detected in kiwi extract, but only one 30-kd allergen has been isolated; it was identified as actinidin (Act c 1). Recently, we have reported a 24-kd kiwi protein to be a potential major allergen in a group of patients with oral allergy syndrome (OAS). Objective: The aim of this study was to purify and characterize the 24-kd kiwi allergen biochemically. Methods: Seven polysensitized patients with OAS to kiwi were used in this study. The kiwi allergen was isolated by using a combination of gel permeation, ion exchange, and immobilized metal ion affinity chromatography. Its biochemical characterization included determination of its isoelectric point, molecular weight, N-terminal sequencing, concanavalin A-binding ability, digestibility in simulated gastric fluid, and antifungal activity. Western blotting, 2-dimensional PAGE immunoblotting, and skin prick tests were performed to characterize the isolated protein immunochemically. Results: All 7 patients recognized the isolated 24-kd kiwi protein as an allergen. The isolated protein consisted of 2 isoforms with isoelectric points of 9.4 and 9.5 migrated as one protein band of 20 kd after SDS-PAGE under nonreducing conditions or at 24 kd under reducing conditions. The partial N-terminal sequence revealed that it is a thaumatin-like protein (TLP) with concanavalin A-binding ability. The protein showed antifungal activity toward Saccharomyces carlsbergensis, and Candida albicans. The protein was degraded by the simulated gastric fluid within 1 minute. Both isoforms bound IgE from a pool of sera in a 2-dimensional PAGE inummoblot. The TLP elicited positive skin prick test responses in 4 (80%) of 5 patients with OAS. Conclusion: This study reported isolation and full characterization of a new kiwi allergen, TLP (isoelectric points of 9.4 and 9.5 and molecular weight of 24 kd), which belongs to the family of pathogenesis-related proteins. The isolated protein expressed antifungal activity toward S carlsbergensis and C albicans. | en |
dc.publisher | Mosby-Elsevier, New York | |
dc.rights | restrictedAccess | |
dc.source | Journal of Allergy and Clinical Immunology | |
dc.subject | allergen purification | en |
dc.subject | antifungal activity | en |
dc.subject | food allergen | en |
dc.subject | kiwi fruit | en |
dc.subject | pathogenesis-related protein | en |
dc.subject | thaumatin-like protein | en |
dc.title | Isolation and biochemical characterization of a thaumatin-like kiwi allergen | en |
dc.type | article | |
dc.rights.license | ARR | |
dc.citation.epage | 810 | |
dc.citation.issue | 5 | |
dc.citation.other | 110(5): 805-810 | |
dc.citation.rank | aM21 | |
dc.citation.spage | 805 | |
dc.citation.volume | 110 | |
dc.identifier.doi | 10.1067/mai.2002.128947 | |
dc.identifier.pmid | 12417892 | |
dc.identifier.scopus | 2-s2.0-0036858690 | |
dc.identifier.wos | 000179082500018 | |
dc.type.version | publishedVersion |