|Liang, X - UNIVERSITY OF GEORGIA|
|Ozias-Akins, P - UNIVERSITY OF GEORGIA|
Submitted to: American Peanut Research and Education Society Abstracts
Publication Type: Abstract Only
Publication Acceptance Date: March 15, 2004
Publication Date: June 10, 2004
Citation: Guo, B., Liang, X. Q., Maleki, S. J., Chung, S. Y., Holbrook, Jr., C. C., Ozias-Akins, P. 2004. Characterization of five seed-proteins missing in one peanut genotype and the allergic nature of these proteins [abstract]. In: Proceedings of the American Peanut Research and Education Society, July 13-16, 2004, San Antonio, Texas. 36:28. Technical Abstract: Food allergies are serious health problems affecting several million people in the United States alone. Researchers are working on several fronts to prevent or reduce peanut allergies. While we were screening for peanut resistance to Aspergillus flavus and aflatoxin contamination and analyzing profiles of peanut seed-storage proteins on 2-D gels, we identified one peanut genotype, GT-C9, lacking 5 proteins in comparison with the other peanut genotypes, Georgia Green, A100, and GT-C20. We have been characterizing and testing these proteins which are missing in one peanut genotype for allergic properties. Five protein spots have been sequenced from 2-D gel of total peanut seed protein extracts using ESI-MS/MS and Edman degradation after trypsin digestion. Based on peptide sequence homology analysis, protein spots labeled as p-1, 2 and 5 are similar to legumin A precursor from Vicia narbonensis, which are essentially the same spectra by both MALDI and ESI, and spot p-3 and 4 are similar to glycinin from Arachis hypogaea, a peanut allergen Ara h3. In collaborating with USDA-ARS, Southern Regional Research Center in New Orleans, the preliminary results of allergenic properties of the total proteins for IgE binding and advanced glycation end adducts (AGEs) show no significant differences among the 4 genotypes. Using more specific antibodies against peanut allergen Ara h1, Ara h2, and Ara h3, Western immunoblotting analyses will shine light on these proteins on 2-D gels. We will conduct N-terminal or C-terminal sequences of these proteins to understand the possible gene structure. The information gained should be useful in breeding peanut cultivars missing the offending allergy-causing proteins through conventional breeding or in developing gene(s)/markers for molecular breeding and genetic transformation to suppress the allergic gene expression.