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United States Department of Agriculture

Agricultural Research Service

Research Project: REDUCING THE ALLERGENIC PROPERTIES OF PEANUTS Title: Bioinformatic tools, resources, and strategies for comparative structural studies of food allergens.

Authors
item Huntley, James -
item Maleki, Soheila
item Baxter, Susan -
item Gonzales, Michael -
item Beavis, William -

Submitted to: Book Chapter
Publication Type: Book / Chapter
Publication Acceptance Date: May 2, 2008
Publication Date: August 10, 2008
Citation: Huntley, J.J., Maleki, S.J., Baxter, S.M., Gonzales, M.D., Beavis, W.D. 2008. Bioinformatic tools, resources, and strategies for comparative structural studies of food allergens. American Society of Microbiology. 322-356.

Interpretive Summary: Legume seed-storage proteins, such as those from soybean and peanut, represent an important source of protein in the human diet. While generally well tolerated, these proteins also represent a potentially serious allergenic threat to many individuals. Despite high sequence similarity of several peanut allergens to their relatively hypoallergenic soy and kidney bean counterparts, it is not well understood why peanuts elicit such an acute allergenic response. We have employed a number of computer software tools and strategies to further investigate the relationship between allergenicity and the amino acid sequence, and structure of legume seed-storage proteins. We find that mapping and comparison of multiple features (sequence conservation among classes, physical location of the amino acids that are bound by allergen–specific antibodies (immunoglobulin E or IgE), and the amino acid residues critical for IgE binding, etc., on known and modeled structures. Our method provides for a better understanding of the relationship between legume protein structure, and the potential for novel legume varieties to elicit reduced allergenic response in the human population.

Technical Abstract: Legume seed-storage proteins, such as those from soybean and peanut, represent an important source of protein in the human diet. While generally well tolerated, these proteins also represent a potentially serious allergenic threat to many individuals. Despite high sequence similarity of several peanut allergens to their relatively hypoallergenic soy and kidney bean counterparts, it is not well understood why peanuts elicit such an acute allergenic response. We have employed a number of bioinformatics tools and strategies to further investigate the relationship between allergenicity and the primary/secondary/tertiary structure of legume seed-storage proteins. We find that mapping and comparison of multiple features (sequence conservation among classes, physical location of IgE epitopes, residues critical for IgE binding, etc.) on known and modeled structures provide for a better understanding of the relationship between legume protein structure, and the potential for novel legume varieties to elicit reduced allergenic response in the human population.

Last Modified: 10/22/2014
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