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Crystal structure of the kiwifruit allergen Act d 5Crystal structure of the kiwifruit allergen Act d 5
Structural highlights
FunctionKIWEL_ACTDE Kissper is an anion-selective pore-forming peptide.[1] Publication Abstract from PubMedKiwellin (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. Elusive Structural, Functional, and Immunological Features of Act d 5, the Green Kiwifruit Kiwellin.,Offermann LR, Giangrieco I, Perdue ML, Zuzzi S, Santoro M, Tamburrini M, Cosgrove DJ, Mari A, Ciardiello MA, Chruszcz M J Agric Food Chem. 2015 Jul 21. PMID:26146952[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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