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IgE-binding potencies of three peach Pru p 1 isoforms.

Authors :: Gao ZS
Zhou X
Yang ZW
Versteeg SA
Gao L
Fu WY
Wang HY
Zhou JY
Akkerdaas JH
van Ree R
Source :: Molecular nutrition & food research [Mol Nutr Food Res] 2016 Nov; Vol. 60 (11), pp. 2457-2466. Date of Electronic Publication: 2016 Sep 12.
Publication Year :: 2016
Abstract: Scope: Pru p 1, the Bet v 1 homologue from peach, has been identified as a clinically relevant allergen. Three isoforms have been described, two in peach fruit (Pru p 1.0101 and Pru p 1.0201) and one in pollen (Pru p 1.0301). The present study aimed to compare their IgE-binding potencies.<br />Methods and Results: Three Pru p 1 isoforms were cloned and expressed as soluble proteins with His-tags in Escherichia coli. Protein identity was confirmed by MS, circular dichroism, and RNAse activity. IgE-binding capacity using ELISA and ImmunoCAP was compared. Three Pru p 1 isoforms had quite similar IgE-binding potencies for 60% of the sera, but more than twofold between any two isoforms among 40% of the 47 sera. The mean IgE binding of Pru p 1.0201 was slightly higher than other two isoforms. In a sera pool, homologous ImmunoCAP inhibition was higher than other two heterologous isoforms. Individual serum with diverse IgE values of three isoforms demonstrated the higher IgE inhibition of specific isoform with higher IgE value.<br />Conclusion: A similar and variable pattern of IgE recognition was observed among three Pru p 1 isoforms. The two new isoforms can be used as more accurate diagnostic reagents.<br /> (© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)