Gojgić, G.

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  • Gojgić, G. (1)
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Isolation and biochemical characterization of a thaumatin-like kiwi allergen

Gavrović-Jankulović, Marija; Ćirković, Tanja; Vučković, Olga; Atanasković-Marković, Marina; Petersen, Arnd; Gojgić, G.; Burazer, Lidija; Jankov, Ratko

(Mosby-Elsevier, New York, 2002)

TY  - JOUR
AU  - Gavrović-Jankulović, Marija
AU  - Ćirković, Tanja
AU  - Vučković, Olga
AU  - Atanasković-Marković, Marina
AU  - Petersen, Arnd
AU  - Gojgić, G.
AU  - Burazer, Lidija
AU  - Jankov, Ratko
PY  - 2002
UR  - http://intor.torlakinstitut.com/handle/123456789/150
AB  - 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.
PB  - Mosby-Elsevier, New York
T2  - Journal of Allergy and Clinical Immunology
T1  - Isolation and biochemical characterization of a thaumatin-like kiwi allergen
EP  - 810
IS  - 5
SP  - 805
VL  - 110
DO  - 10.1067/mai.2002.128947
UR  - conv_136
ER  - 
@article{
author = "Gavrović-Jankulović, Marija and Ćirković, Tanja and Vučković, Olga and Atanasković-Marković, Marina and Petersen, Arnd and Gojgić, G. and Burazer, Lidija and Jankov, Ratko",
year = "2002",
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.",
publisher = "Mosby-Elsevier, New York",
journal = "Journal of Allergy and Clinical Immunology",
title = "Isolation and biochemical characterization of a thaumatin-like kiwi allergen",
pages = "810-805",
number = "5",
volume = "110",
doi = "10.1067/mai.2002.128947",
url = "conv_136"
}
Gavrović-Jankulović, M., Ćirković, T., Vučković, O., Atanasković-Marković, M., Petersen, A., Gojgić, G., Burazer, L.,& Jankov, R.. (2002). Isolation and biochemical characterization of a thaumatin-like kiwi allergen. in Journal of Allergy and Clinical Immunology
Mosby-Elsevier, New York., 110(5), 805-810.
https://doi.org/10.1067/mai.2002.128947
conv_136
Gavrović-Jankulović M, Ćirković T, Vučković O, Atanasković-Marković M, Petersen A, Gojgić G, Burazer L, Jankov R. Isolation and biochemical characterization of a thaumatin-like kiwi allergen. in Journal of Allergy and Clinical Immunology. 2002;110(5):805-810.
doi:10.1067/mai.2002.128947
conv_136 .
Gavrović-Jankulović, Marija, Ćirković, Tanja, Vučković, Olga, Atanasković-Marković, Marina, Petersen, Arnd, Gojgić, G., Burazer, Lidija, Jankov, Ratko, "Isolation and biochemical characterization of a thaumatin-like kiwi allergen" in Journal of Allergy and Clinical Immunology, 110, no. 5 (2002):805-810,
https://doi.org/10.1067/mai.2002.128947 .,
conv_136 .
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