Expression, purification and crystallization of pecan (Carya illinoinensis) vicilin

Acta Crystallogr F Struct Biol Commun. 2014 Aug;70(Pt 8):1049-52. doi: 10.1107/S2053230X14012369. Epub 2014 Jul 23.

Abstract

Tree nuts are responsible for many cases of severe food allergies. The 7S seed storage protein vicilin has been identified as a food allergen in many kinds of tree nuts. The vicilin protein consists of an N-terminal low-complexity region with antimicrobial activity and a C-terminal domain that forms a trimeric structure that belongs to the cupin superfamily. In this study, vicilin from pecan (Carya illinoinensis) was isolated and was expressed in bacteria for the first time. The cupin structural core of the protein, residues 369-792, was purified by metal-affinity and gel-filtration chromatography to high purity. Vicilin crystals were obtained and the best crystal diffracted to 2.65 Å resolution in space group P212121.

Keywords: Carya illinoinensis; convicilin; food allergen; storage protein.

MeSH terms

  • Base Sequence
  • Carya / chemistry*
  • Chromatography, Affinity
  • Chromatography, Gel
  • Crystallization
  • DNA Primers
  • Seed Storage Proteins / chemistry
  • Seed Storage Proteins / genetics*
  • Seed Storage Proteins / isolation & purification

Substances

  • DNA Primers
  • Seed Storage Proteins
  • vicilin protein, plant