Cloning, Expression, and Characterization of Ara h 3, a Major Peanut Allergen

<p>Abstract There are eight foods that contribute to food allergies in the western world and peanut is the most common. Currently, there are no medical treatments that can cure an individual of food allergy, so avoidance of the allergic food is the only option. In the United States, there are three immunodominant allergic proteins accountable for patient sensitization to peanut, Arachis hypogea 1, 2, and 3 (Ara h 1, Ara h 2, Ara h 3). Therefore, research into why peanuts are more allergic than other foods that have homologous proteins is critical and may be obtained by studying the structural and allergenic properties of individual allergens and the changes that occur due to food processing. In this study, the basic and acidic subunits of Ara h 3 were cloned, expressed, and purified, and compared with each other and with the native Ara h 3 purified from peanut for differences in binding to IgE from peanut allergic individuals. Also, an in vitro Maillard reaction was performed on purified native raw Ara h 3 and patient serum IgE western blots were performed. This study concluded that an in vitro Maillard reaction enhanced IgE binding to Ara h 3, IgE binding to native Ara h 3 was in most cases higher than to the recombinant Ara h 3 subunits, and recognition of the acidic subunit was much higher than the and basic subunits in both the recombinant and native forms of the protein were investigated. Keywords:</p>

Name thesis:degree_name

M.S.

Level thesis:degree_level

Thesis

Discipline thesis:degree_discipline

Biological Sciences

Year dc:date.available

2012

Author dc:creator

• Garvey, Cathryn E.

Contributors dc:contributor

• Wendy Schluchter
• Soheila J. Maleki
• Zhengchang Liu

• Peanut Allergy, Ara h 3, Allergic Reaction, Immunoglobulin E (IgE), Antigen, Sensitization, FcεRI Receptor, Epitope, Mast Cell, Maillard Reaction, Simulated Roasted Model (SRM), Simulated Roasted (SR)
• Biochemistry
• Food Biotechnology
• Food Chemistry
• Food Microbiology
• Molecular Biology
• Other Immunology and Infectious Disease
• Structural Biology

Repository record dc:identifier

https://scholarworks.uno.edu/td/1565

OAI identifier oai:identifier

oai:scholarworks.uno.edu:td-2640