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Ara h1
Ara h 1 is a seed storage protein from ''Arachis hypogaea'' (peanuts). It is a heat stable 7S vicilin-like globulin〔Wichers HJ, De Beijer T, Savelkoul HF, Van Amerongen A. The major peanut allergen Ara h 1 and its cleaved-off N-terminal peptide; possible implications for peanut allergen detection. J Agric Food Chem 2004;52(15):4903-7〕 with a stable trimeric form〔Pomes A, Helm RM, Bannon GA, Burks AW, Tsay A, Chapman MD. Monitoring peanut allergen in food products by measuring Ara h 1. J Allergy Clin Immunol 2003;111(3):640-5〕 that comprises 12-16% of the total protein in peanut extracts.〔de Jong EC, Van Zijverden M, Spanhaak S, Koppelman SJ, Pellegrom H, Penninks AH. Identification and partial characterization of multiple major allergens in peanut proteins. Clin Exp Allergy 1998;28(6):743-51〕 Ara h 1 is known because sensitization to it was found in 95% of peanut-allergic patients from North America. In spite of this high percentage, peanut-allergic patients of European populations have fewer sensitizations to Ara h 1.〔Saavedra-Delgado AM. The many faces of the peanut. Allergy Proc 1989;10(4):291-4〕
==Structure==
Ara h 1 is a vicilin, located in the protein fraction of the peanut cotyledon.〔Bush, R. K, S. L. Taylor, J. A. Nordlee. 1989. Peanut sensitivity. Allergy Proc. 10: 261〕〔Taylor, S. L., W. W. Busse, M. I. Sachs, J. L. Parker, J. W. Yunginger. 1981. Peanut oil is not allergenic to peanut-sensitive individuals. J. Allergy Clin. Immunol. 68: 372〕 Ara h 1 forms homotrimers, and due to its highly stable structure, mediated through hydrophobic interactions, it has been established as an allergen.〔Shin, D., C. M. Compadre, S. J. Maleki, R. A. Kopper, H. Sampson, S. K. Huang, A. W. Burks, G. A. Bannon. 1998. Biochemical and structural analysis of the IgE binding sites on Ara h 1, an abundant and highly allergenic peanut protein. J. Biol. Chem. 273: 13753〕
Hydrophobic residues on α-helical bundles are located on the ends of each trimer monomer. Ara h 1 presents an overall pleat like bicupins, N- and C-terminal domains are superposed in 1.9 Å. The molecule has two modules related by an axis perpendicular to the three pleat axes of the trimer. They interact through their hydrophobic parts. The trimeric assemblies are stabilized by multiple hydrogen bonds.
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