Solution structure of the strawberry allergen Fra a 1

Biosci Rep. 2012 Dec;32(6):567-75. doi: 10.1042/BSR20120058.


The PR10 family protein Fra a 1E from strawberry (Fragaria x ananassa) is down-regulated in white strawberry mutants, and transient RNAi (RNA interference)-mediated silencing experiments confirmed that Fra a 1 is involved in fruit pigment synthesis. In the present study, we determined the solution structure of Fra a 1E. The protein fold is identical with that of other members of the PR10 protein family and consists of a seven-stranded antiparallel β-sheet, two short V-shaped α-helices and a long C-terminal α-helix that encompass a hydrophobic pocket. Whereas Fra a 1E contains the glycine-rich loop that is highly conserved throughout the protein family, the volume of the hydrophobic pocket and the size of its entrance are much larger than expected. The three-dimensional structure may shed some light on its physiological function and may help to further understand the role of PR10 proteins in plants.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antigens, Plant / chemistry*
  • Chromatography, Gel
  • Circular Dichroism
  • Fragaria / chemistry*
  • Hydrophobic and Hydrophilic Interactions
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular
  • Plant Proteins / chemistry*
  • Protein Conformation


  • Antigens, Plant
  • Fra a 1 allergen, Fragaria ananassa
  • Plant Proteins