Crystal Structure of Cocosin, A Potential Food Allergen from Coconut (Cocos nucifera)

J Agric Food Chem. 2017 Aug 30;65(34):7560-7568. doi: 10.1021/acs.jafc.7b02252. Epub 2017 Jul 31.

Abstract

Coconut (Cocos nucifera) is an important palm tree. Coconut fruit is widely consumed. The most abundant storage protein in coconut fruit is cocosin (a likely food allergen), which belongs to the 11S globulin family. Cocosin was crystallized near a century ago, but its structure remains unknown. By optimizing crystallization conditions and cryoprotectant solutions, we were able to obtain cocosin crystals that diffracted to 1.85 Å. The cocosin gene was cloned from genomic DNA isolated from dry coconut tissue. The protein sequence deduced from the predicted cocosin coding sequence was used to guide model building and structure refinement. The structure of cocosin was determined for the first time, and it revealed a typical 11S globulin feature of a double layer doughnut-shaped hexamer.

Keywords: 11S globulin; coconut; cocosin; food allergen; hexameric structure.

MeSH terms

  • Allergens / chemistry*
  • Allergens / genetics
  • Allergens / immunology
  • Amino Acid Sequence
  • Cocos / chemistry
  • Cocos / genetics
  • Cocos / immunology*
  • Crystallization
  • Crystallography, X-Ray
  • Molecular Sequence Data
  • Plant Proteins / chemistry*
  • Plant Proteins / genetics
  • Plant Proteins / immunology

Substances

  • Allergens
  • Plant Proteins