Effect of deglycosylation on immunoreactivity and  in vitro  pepsin digestibility of major cashew ( Anacardium occidentale  L.) allergen, Ana o 1 | Zendy

Zaffran Valerie D. | Zendy; Gupta Sahil | Zendy; Sathe Shridhar K. | Zendy; Roper Michael G. | Zendy

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Effect of deglycosylation on immunoreactivity and in vitro pepsin digestibility of major cashew ( Anacardium occidentale L.) allergen, Ana o 1

Author(s) -

Zaffran Valerie D.,

Gupta Sahil,

Sathe Shridhar K.,

Roper Michael G.

Publication year - 2021

Publication title -

journal of food science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.772

H-Index - 150

eISSN - 1750-3841

pISSN - 0022-1147

DOI - 10.1111/1750-3841.15628

Subject(s) - anacardium , chemistry , allergen , hypoallergenic , pepsin , glycosylation , immunoglobulin e , in vitro , digestion (alchemy) , biochemistry , glycan , antibody , epitope , enzyme , glycoprotein , allergy , chromatography , immunology , biology , horticulture

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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