Location: Food Processing and Sensory Quality Research
Title: Modification of purified Ana o 3 with phenylglyoxal disrupts antibody bindingAuthor
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Brown, Chaka |
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Dupre, Rebecca |
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Vuong, Tien |
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PAYNE, ALEXIS - Oak Ridge Institute For Science And Education (ORISE) |
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Smith, Brennan |
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Mattison, Christopher |
Submitted to: Meeting Abstract
Publication Type: Abstract Only Publication Acceptance Date: 5/21/2024 Publication Date: N/A Citation: N/A Interpretive Summary: Technical Abstract: Ana o 3 is an immunodominant cashew nut allergen, and immunoglobulin (IgE) antibodies to Ana o 3 are strong predictors for clinically relevant cashew allergy and severe allergic reaction. Four mouse monoclonal anti-Ana o 3 antibodies have been characterized, and in silico docking experiments predict two conformational epitopes and two linear epitopes. The 2H5 and 5B7F8 clones recognize linear Ano 3 epitopes that are not disrupted by treatment of purified Ana o 3 with a reducing agent such as dithiothreitol. The predicted 2H5 and 5B7F8 epitopes lie within published linear Ana o 3-IgE epitopes and include arginine residues R21, R28, R30, R42, and R45. Phenylgloxal (PG) has been used to selectively modify arginine residues on protein surfaces and within active sites. Here, purified Ana o 3 is chemically modified with PG, and we demonstrate that this modification reduces 2H5 and 5B7F8 antibody binding to Ana o 3. The findings are consistent with in silico modeling predictions and suggest that surface exposed arginine residues are, at least in part, important for 2H5 and 5B7F8 monoclonal anti-Ana o 3 antibody binding. |