An FKBP destabilization domain modulates protein levels in Plasmodium falciparum

Nat Methods. 2007 Dec;4(12):1007-9. doi: 10.1038/nmeth1132. Epub 2007 Nov 11.


To enhance the repertoire of molecular tools for studying malaria parasite biology, we adapted a ligand-regulatable FKBP protein destabilization domain (ddFKBP) for use in P. falciparum. We destabilized the reporter yellow fluorescent protein (YFP) and the P. falciparum protease falcipain-2 in a ligand-reversible manner by tagging with ddFKBP. The swollen food vacuole phenotype of falcipain-2 knockout parasites could be rescued in a Shld1 ligand-dependent fashion by falcipain-2-ddFKBP expression.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Gene Expression Regulation / physiology*
  • Gene Silencing*
  • Gene Targeting / methods
  • Genetic Engineering / methods*
  • Plasmodium falciparum / genetics*
  • Protein Structure, Tertiary
  • Protozoan Proteins / chemistry
  • Protozoan Proteins / genetics*
  • Tacrolimus Binding Proteins / chemistry
  • Tacrolimus Binding Proteins / genetics*
  • Toxoplasma / genetics*


  • Protozoan Proteins
  • Tacrolimus Binding Proteins