Changes in the antigenicity and allergenicity of ovalbumin in chicken egg white by N-acetylglucosaminidase

• Published in: Food chemistry Vol. 217; pp. 342 - 345
• Main Authors: Park, Ho-Young, Yoon, Taek Joon, Kim, Ha Hyung, Han, Young Shin, Choi, Hee-Don
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 15.02.2017
• Subjects: Acetylglucosaminidase - metabolism; Allergenicity; Allergens - chemistry; Allergens - immunology; Animals; Antigenicity; Child, Preschool; Egg white; Egg White - chemistry; Female; Glycosylation; Histamine - blood; Histamine - immunology; Humans; Immunoglobulin E - blood; Immunoglobulin E - immunology; Infant; Male; Mice; Mice, Inbred BALB C; N-Acetylglucosaminidase; Ovalbumin; Ovalbumin - chemistry; Ovalbumin - immunology; Ovalbumin; N-Acetylglucosaminidase; Egg white; Antigenicity; Allergenicity
• ISSN: 0308-8146; 1873-7072
• DOI: 10.1016/j.foodchem.2016.08.112

•N-OVA significantly OVA-specific IgE and histamine levels.•N-OVA decreased the antigenicity of OVA 1000-fold.•Allergenicity and antigenicity are reduced by N-acetylglucosaminidase in OVA. Ovalbumin (OVA), an (hen) egg allergen, is one of the most abundant glycoprotein allergens associated with IgE-mediated hypersensitivity through the T-helper type 2 immune response. The effect of deglycosylation of the N-terminal glycan in OVA on allergenicity and antigenicity after N-acetylglucosaminidase treatment was studied. N-acetylglucosaminidase-treated OVA (N-OVA) evaluated using an enzyme-linked immunosorbent assay, respectively. N-OVA significantly (p<0.05) OVA-specific IgE and histamine levels. In addition, N-OVA decreased the antigenicity of OVA 1000-fold. These results suggest that the degree of allergenicity and antigenicity reduced with deglycosylation of N-terminal glycan in OVA.