TY - JOUR
T1 - Elusive Structural, Functional, and Immunological Features of Act d 5, the Green Kiwifruit Kiwellin
AU - Offermann, Lesa R.
AU - Giangrieco, Ivana
AU - Perdue, Makenzie L.
AU - Zuzzi, Sara
AU - Santoro, Mario
AU - Tamburrini, Maurizio
AU - Cosgrove, Daniel J.
AU - Mari, Adriano
AU - Ciardiello, Maria Antonietta
AU - Chruszcz, Maksymilian
N1 - Publisher Copyright:
© 2015 American Chemical Society.
PY - 2015/7/29
Y1 - 2015/7/29
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84938399992&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84938399992&partnerID=8YFLogxK
U2 - 10.1021/acs.jafc.5b02159
DO - 10.1021/acs.jafc.5b02159
M3 - Article
C2 - 26146952
AN - SCOPUS:84938399992
SN - 0021-8561
VL - 63
SP - 6567
EP - 6576
JO - Journal of agricultural and food chemistry
JF - Journal of agricultural and food chemistry
IS - 29
ER -