| Literature DB >> 26146952 |
Lesa R Offermann1, Ivana Giangrieco2, Makenzie L Perdue1, Sara Zuzzi3,4, Mario Santoro3,4, Maurizio Tamburrini2, Daniel J Cosgrove5, Adriano Mari3,4, Maria Antonietta Ciardiello2, Maksymilian Chruszcz1.
Abstract
Kiwellin (Act d 5) is an allergenic protein contained in kiwifruit pulp in high amounts. The aim of this study was to investigate the three-dimensional structure of the natural molecule from green kiwifruit and its possible function. Kiwellin was crystallized, and its structure, including post-translational modifications, was elucidated. The molecular weight and structural features, in solution, were analyzed by gel filtration and circular dichroism, respectively. Although structurally similar to expansin, kiwellin lacks expansin activity and carbohydrate binding. A specific algorithm was applied to investigate any possible IgE reactivity correlation between kiwellin and a panel of 102 allergens, including expansins and other carbohydrate-binding allergens. The available data suggest a strong dependence of the kiwellin structure on the environmental/experimental conditions. This dependence therefore poses challenges in detecting the correlations between structural, functional, and immunological features of this protein.Entities:
Keywords: allergen; kiwellin; kiwifruit; protein crystallization
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Year: 2015 PMID: 26146952 DOI: 10.1021/acs.jafc.5b02159
Source DB: PubMed Journal: J Agric Food Chem ISSN: 0021-8561 Impact factor: 5.279