Crystal structure of peanut (Arachis hypogaea) allergen Ara h 5.
Profilins from numerous species are known to be allergens, including food allergens, such as peanut ( Arachis hypogaea ) allergen Ara h 5, and pollen allergens, such as birch allergen Bet v 2. Patients with pollen allergy can also cross-react to peanut. Structural characterization of allergens will allow a better understanding of the allergenicity of food allergens and their cross-reactivities. The three-dimensional structures of most known food allergens remain to be elucidated. Here, we report the first crystallographic study of a food allergen in the profilin family. The structure of peanut allergen Ara h 5 was determined, and the resolution of the final refined structure was 1.1 Å. Structure alignment revealed that Ara h 5 is more similar to Bet v 2 than to Hev b 8, although sequence alignment suggested that Ara h 5 is more closely related to Hev b 8 than to Bet v 2, indicating that homology-model-based prediction of immunoglobulin E epitopes needs to be interpreted with caution.
Department of Biological and Chemical Sciences, Illinois Institute of Technology, Chicago, Illinois 60616, United States.
Yang
Y
Wang
Tong-Jen
TJ
Fu
Andrew
A
Howard
Mahendra H
MH
Kothary
Tara H
TH
McHugh
Yuzhu
Y
Zhang
D000485:Allergens / Q000737:chemistry*; D052179:Antigens, Plant / Q000737:chemistry*; D010367:Arachis / Q000737:chemistry*; D002852:Chromatography, Ion Exchange; D006023:Glycoproteins / Q000737:chemistry*; D015394:Molecular Structure; D010940:Plant Proteins / Q000737:chemistry*; D051304:Profilins / Q000737:chemistry*; D017433:Protein Structure, Secondary
D000485:Allergens; D052179:Antigens, Plant; D006023:Glycoproteins; D010940:Plant Proteins; D051304:Profilins