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1.  Purification and crystallization of Cor a 9, a major hazelnut allergen 
The major hazelnut allergen Cor a 9 was purified from the natural source and crystallized. Diffraction data were collected to 1.9 Å resolution using a synchrotron-radiation source.
Hazelnut (Corylus avellana) is one of the food sources that induce allergic reaction in a subpopulation of people with food allergy. The 11S legumin-like seed-storage protein from hazelnut has been identified as one of the major hazelnut allergens and named Cor a 9. In this study, Cor a 9 was extracted from hazelnut kernels using a high-salt solution and was purified by desalting out and FPLC to a highly purified state. Diffraction-quality single crystals were obtained using the hanging-drop vapour-diffusion method. Diffraction data were collected and a structure solution has been obtained by molecular-replacement calculations. Further refinement of the structure is currently in progress.
doi:10.1107/S1744309108039894
PMCID: PMC2628846  PMID: 19153454
hazelnuts; 11S seed-storage proteins; food allergies; tree-nut allergens
2.  Crystallization and initial crystallographic characterization of a vicilin-type seed storage protein from Pinus koraiensis  
In this study, the Korean pine (Pinus koraiensis) vicilin-type 7S seed storage protein was isolated from defatted pine-nut extract and purified by sequential gel-filtration and anion-exchange chromatography. Well diffracting single crystals were obtained by the vapour-diffusion method in hanging drops.
The cupin superfamily of proteins includes the 7S and 11S seed storage proteins. Many members of this family of proteins are known allergens. In this study, the Korean pine (Pinus koraiensis) vicilin-type 7S seed storage protein was isolated from defatted pine-nut extract and purified by sequential gel-filtration and anion-exchange chromatography. Well diffracting single crystals were obtained by the vapor-diffusion method in hanging drops. The crystals belong to the primitive cubic space group P213, with unit-cell parameters a = b = c = 148.174 Å. Two vicilin molecules were present in the asymmetric unit and the Matthews coefficient was determined to be 2.90 Å3 Da−1, with a corresponding solvent content of ∼58%. A molecular-replacement structural solution has been obtained using the program Phaser. Refinement of the structure is currently under way.
doi:10.1107/S1744309107054310
PMCID: PMC2344101  PMID: 18084088
allergens; pine nuts; seed storage protein
3.  Protein digestibility and relevance to allergenicity. 
Environmental Health Perspectives  2003;111(8):1122-1124.
In January 2001 a Joint Food and Agriculture Organization of the United Nations/World Health Organization Expert Consultation Committee on Allergenicity of Foods Derived from Biotechnology published a report outlining in detail an approach for assessing the allergenic potential of novel proteins. One component of this decision tree is a determination of whether the protein of interest is resistant to proteolytic digestion. Although these (Italic)in vitro(/Italic) methodologies have been useful, the correlation between resistance to proteolysis and allergenic activity is not absolute. Two views and highlights of supporting research regarding the relationship of resistance to digestion and allergenicity are presented in this article.
PMCID: PMC1241561  PMID: 12826484

Results 1-3 (3)