Elusive Structural, Functional, and Immunological Features of Act d 5, the Green Kiwifruit Kiwellin

被引:22
|
作者
Offermann, Lesa R. [1 ]
Giangrieco, Ivana [2 ]
Perdue, Makenzie L. [1 ]
Zuzzi, Sara [3 ,4 ,5 ]
Santoro, Mario [3 ,4 ,5 ]
Tamburrini, Maurizio [2 ]
Cosgrove, Daniel J. [6 ]
Mari, Adriano [3 ,4 ,5 ]
Ciardiello, Maria Antonietta [2 ]
Chruszcz, Maksymilian [1 ]
机构
[1] Univ S Carolina, Dept Chem & Biochem, Columbia, SC 29208 USA
[2] CNR, Inst Biosci & Bioresources, I-80131 Naples, Italy
[3] IDI IRCCS, Ctr Mol Allergol, Rome, Italy
[4] Associated Ctr Mol Allergol, Rome, Italy
[5] Associated Ctr Mol Allergol, Latium, Italy
[6] Penn State Univ, Dept Biol, University Pk, PA 16802 USA
关键词
kiwellin; kiwifruit; allergen; protein crystallization; KIWI FRUIT PEPTIDE; X-RAY-DIFFRACTION; CELL-WALL; CRYSTAL-STRUCTURE; IN-VITRO; PROTEIN; MODEL; REACTIVITY; CONSERVATION; PURIFICATION;
D O I
10.1021/acs.jafc.5b02159
中图分类号
S [农业科学];
学科分类号
09 ;
摘要
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.
引用
收藏
页码:6567 / 6576
页数:10
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