title: Structural and Functional Characterization of the Hazelnut Allergen Cor a 8.
abstract: Nonspecific lipid transfer proteins (nsLTPs) are basic proteins, stabilized by four disulfide bonds, and are expressed throughout the plant kingdom. These proteins are also known as important allergens in fruits and tree nuts. In this study, the nsLTP from hazelnuts, Cor a 8, was purified and its crystal structure determined. The protein is stable at low pH and refolds after thermal denaturation. Molecular dynamics simulations were used to provide an insight into conformational changes of Cor a 8 upon ligand binding. When known epitope areas from Pru p 3 were compared to those of Cor a 8, differences were obvious, which may contribute to limited cross-reactivity between peach and hazelnut allergens. Differences in epitope regions may contribute to limited cross-reactivity between Cor a 8 and nsLTPs from other plant sources. The structure of Cor a 8 represents the first resolved structure of a hazelnut allergen.
authors.affiliation: Department of Chemistry and Biochemistry, University of South Carolina , Columbia, South Carolina 29208, United States.|Department of Chemistry, Davidson College , Davidson, North Carolina 28035, United States.
authors.forename: Lesa R
authors.initials: LR
authors.lastname: Offermann
authors.affiliation: Department of Pathophysiology and Allergy Research, Center for Pathophysiology, Infectiology and Immunology, Medical University of Vienna , Vienna, Austria.
authors.forename: Merima
authors.initials: M
authors.lastname: Bublin
authors.affiliation: Department of Chemistry and Biochemistry, University of South Carolina , Columbia, South Carolina 29208, United States.
authors.forename: Makenzie L
authors.initials: ML
authors.lastname: Perdue
authors.affiliation: Department of Pathophysiology and Allergy Research, Center for Pathophysiology, Infectiology and Immunology, Medical University of Vienna , Vienna, Austria.
authors.forename: Sabine
authors.initials: S
authors.lastname: Pfeifer
authors.affiliation: Department of Pathophysiology and Allergy Research, Center for Pathophysiology, Infectiology and Immunology, Medical University of Vienna , Vienna, Austria.
authors.forename: Pawel
authors.initials: P
authors.lastname: Dubiela
authors.affiliation: Jerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences , Kraków, Poland.
authors.forename: Tomasz
authors.initials: T
authors.lastname: Borowski
authors.affiliation: Department of Chemistry and Biochemistry, University of South Carolina , Columbia, South Carolina 29208, United States.
authors.forename: Maksymilian
authors.initials: M
authors.lastname: Chruszcz
authors.affiliation: Department of Pathophysiology and Allergy Research, Center for Pathophysiology, Infectiology and Immunology, Medical University of Vienna , Vienna, Austria.
authors.forename: Karin
authors.initials: K
authors.lastname: Hoffmann-Sommergruber
mesh_terms: D000485:Allergens / Q000737:chemistry* / Q000276:immunology*; D052179:Antigens, Plant / Q000737:chemistry* / Q000276:immunology*; D031211:Corylus / Q000737:chemistry*; D003429:Cross Reactions; D018360:Crystallography, X-Ray; D000939:Epitopes / Q000737:chemistry / Q000276:immunology; D010940:Plant Proteins / Q000737:chemistry* / Q000276:immunology*
chemical_list: D000485:Allergens; D052179:Antigens, Plant; D000939:Epitopes; D010940:Plant Proteins
keywords: allergen; food allergy; hazelnut; nonspecific lipid transfer protein; protein crystallization