Tertiary structure and biophysical properties of a major peanut allergen, implications for the production of a hypoallergenic protein

International Archives of Allergy and Immunology

Volumn 118, Issue 2-4, 1999, Pages 315-316

  Bannon, Gary A ^a   Shin, David ^a   Maleki, Soheila ^a   Kopper, Randall ^a   Burks, A Wesley ^a  

^a UNIVERSITY OF ARKANSAS FOR MEDICAL SCIENCES   (United States)

Author keywords

Hypoallergenic; IgE; Peanut allergen; Structure

Indexed keywords

ALLERGEN; IMMUNOGLOBULIN E;

ALLERGENICITY; AMINO ACID SUBSTITUTION; CONFERENCE PAPER; HYDROPHOBICITY; HYPERSENSITIVITY; NONHUMAN; PEANUT; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE;

EID: 0032916159     PISSN: 10182438     EISSN: None     Source Type: Journal    
DOI: 10.1159/000024115     Document Type: Conference Paper

References (5)

1. Burks AW, Williams LW, Connaughton C, Cockrell G, O'Brien T, Helm RM: Identification of a major peanut allergen. Ara h I, in patients with atopic dermatitis and positive peanut challenges. J Allergy Clin Immunol 1991;88:172-179.
2. Burks AW, Cockrell G, Stanley JS, Helm RM, Bannon GA: Recombinant peanut allergen Ara h I expression and IgE binding in patients with peanut hypersensitivity. J Clin Invest 1995;96: 1715-1721.
3. Burks AW, Shin D, Cockrell G, Stanley JS, Helm RM, Bannen GA: Mapping and mutational analysis of the IgE binding epitopes on Ara h 1, a legume vicilin protein and a major allergen in peanut hypersensitivity. Eur J Biol 1997;245:334-339.
4. Shin D, Compadre CM, Maleki SJ, Kopper RA, Sampson H, Huang SK, Burks AW, Bannon GA: Biochemical and structural analysis of the IgE binding sites on Ara h 1, an abundant and highly allergenic peanut protein. J Biol Chem 1998;273:13753-13759.
5. Lawrence MC, Izard T, Beuchat M, Blagrove RJ, Colman PM: Structure of phaseolin at 2.2 A resolution. Implications for a common vicilin/legumin structure and the genetic engineering of seed storage proteins. J Mol Biol 1994;238:748-776.