Title
IgE-binding potencies of three peach Pru p 1 isoforms
Author
Zhong-shan Gao, Xiang Zhou, Zhao-wei Yang, Serge A. Versteeg, Ling Gao, Wan-yi Fu, Hui-ying Wang, Jian-ying Zhou, Jaap H. Akkerdaas, Ronald van Ree
Year
2016
Journal
Molecular Nutrition & Food Research
Abstract
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, Pru
p 1.0201) and one in pollen (Pru p 1.0301). The present study aimed to compare their IgE
binding potencies. Three Pru p 1 isoforms were cloned and expressed as soluble proteins
with His-tags in Escherichia coli. Protein identity was confirmed by mass spectrometry,
circular dichroism, and RNAse activity. IgE binding capacity by ELISA and ImmunoCAP was
compared. Three Pru p 1 isoforms had quite similar IgE-binding potencies for 60% of the
sera, but more than two-fold 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. 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.
Instrument
J-810
Keywords
Circular dichroism, Secondary structure, Biochemistry, Food science