Elusive Structural, Functional, and Immunological Features of Act d 5, the Green Kiwifruit Kiwellin
Author(s) -
L.R. Offermann,
Ivana Giangrieco,
M.L. Perdue,
Sara Zuzzi,
Mario Santoro,
Maurizio Tamburrini,
Daniel J. Cosgrove,
Adriano Mari,
Maria Antonietta Ciardiello,
M. Chruszcz
Publication year - 2015
Publication title -
journal of agricultural and food chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.203
H-Index - 297
eISSN - 1520-5118
pISSN - 0021-8561
DOI - 10.1021/acs.jafc.5b02159
Subject(s) - expansin , circular dichroism , chemistry , carbohydrate , biochemistry , size exclusion chromatography , protein structure , biophysics , biology , enzyme , gene expression , gene
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.
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