Effect of deglycosylation on immunoreactivity and in vitro pepsin digestibility of major cashew (Anacardium occidentale L.) allergen, Ana o 1
Zaffran, V. D., Gupta, S., Sathe, S. K., & Roper, M. G.
Major cashew allergen, Ana o 1, was purified in its native form from cashew seeds and subjected to enzymatic deglycosylation using PNGase F to assess the potential role of N-glycans in immunoreactivity. Western and dot blotting with pooled human plasma containing anticashew IgE revealed that deglycosylation increased IgE-binding of Ana o 1. Removal of N-glycans may have exposed previously masked Ana o 1 epitopes. Purified glycosylated and deglycosylated Ana o 1 were also subjected to in vitro pepsin digestion at pH 3.0 for 2 hr. Both glycosylated and deglycosylated Ana o 1 remained stable and reactive with IgE antibodies following digestion. PRACTICAL APPLICATION: Understanding the role of glycosylation in Ana o 1 immunoreactivity may provide insight into the potential development of hypoallergenic cashews/cashew products for sensitive individuals in the future.
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