Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 63, Issue 41, Pages 9150-9158Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.5b03534
Keywords
allergen; food allergy; hazelnut; nonspecific lipid transfer protein; protein crystallization
Funding
- ASPIRE grant from the Office of the Vice President of Research at the University of South Carolina
- Austrian Science Fund (FWF) [SFB F4603, W1248]
- PL-Grid Infrastructure
- Austrian Science Fund (FWF) [W1248] Funding Source: Austrian Science Fund (FWF)
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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 Pm 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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