Open AccessStructural and Functional Characterization of the Hazelnut Allergen Cor a 8
Author(s) -
L.R. Offermann,
Merima Bublin,
M.L. Perdue,
Sabine Pfeifer,
Paweł Dubiela,
Tomasz Borowski,
M. Chruszcz,
Karin HoffmannSommergruber
Publication year - 2015
Publication title -
journal of agricultural and food chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.203
H-Index - 297
eISSN - 1520-5118
pISSN - 0021-8561
DOI - 10.1021/acs.jafc.5b03534
Subject(s) - plant lipid transfer proteins , chemistry , epitope , allergen , cross reactivity , denaturation (fissile materials) , protein structure , reactivity (psychology) , biochemistry , allergy , cross reactions , antigen , biology , immunology , medicine , alternative medicine , pathology , nuclear chemistry , gene
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.
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