Recombinant peanut allergen Ara h I expression and IgE binding in patients with peanut hypersensitivity. (1)
During the course of sequencing it was noted that fraction I and III consisted of a single peptide species (peptide I and peptide III, respectively).
This insert hybridized to an- 2.3-kb mRNA indicating that this insert probably represented the entire mRNA.
The IgE pool recognized whole peanut extract and purified native Ara h I protein as expected, but did not react with any proteins from an E. coli lysate that was prepared from cells carrying vector alone.
Of the 18 patient sera tested in this manner there were varying intensities of IgE binding to the recombinant and native allergen.
The major peanut allergens are vicilin-like proteins may explain why patients with peanut hypersensitivity and peanut-specific IgE tend to have serum IgE to multiple other legume proteins. Since the vicilins of most major plants share significant sequence homology in their carboxy terminal portion, it is not surprising that serum specific IgE would tend to bind to several vicilin proteins from different sources.