Identification of actinidin as the major allergen of kiwi fruit☆,☆☆,★
Section snippets
Kiwi-sensitive patients
A pool of sera from 30 patients with allergic symptoms to kiwi who were positive for kiwi-specific IgE antibodies was used to check the in vitro IgE-binding capacity of the fractions of kiwi purified from the crude extract. The patients' clinical characteristics, the results of oral provocation tests with kiwi, and the levels of kiwi-specific IgE for each patient have been reported fully elsewhere.5 The sera of seven of these 30 patients were used to check the IgE immunoblotting of kiwi in
HPLC and SDS-PAGE/immunoblotting
Pilot experiments were conducted with the Resource Q (1 ml) anion-exchange column connected to the HPLC system to establish the optimal buffer system and salt gradient (linear from 0 to 0.5 mol/L of NaCl). This procedure, conducted on a concentrated kiwi extract of 11 mg/ml (the unconcentrated extract had too low a protein concentration), led to the separation of four peaks (Fig. 1, A), which, analyzed in SDS-PAGE, showed good purification. FIG.1. Anion-exchange chromatogram of crude kiwi
Discussion
This study provides evidence that actinidin is the major allergen of the fruit Actinidia chinensis, commonly called kiwi. Theoretically, this should not be surprising because actinidin accounts for about 50% of the soluble proteins of the fruit. However, we did not imagine this when, in a previous study, we identified the major allergen of kiwi as a 30 kd band because actinidin was reported in 1978 as an enzymatic protein of 23.5 kd.14 The apparent MW of nearly 30 kd obtained from the sodium
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From athe third Department of General Medicine, Ospedale Maggiore IRCCS, Milan; bBizzozzero Division, Niguarda Ca' Granda Hospital, Milan; and cthe National Research Council, Torino.
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Reprint requests: Elide A. Pastorello, MD, Ospedale Maggiore di Milano, IRCCS, Pad. Granelli, Via F. Sforza 35, 20122 Milan, Italy.
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