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An FKBP destabilization domain modulates protein levels in Plasmodium falciparum
Christopher M Armstrong1, Daniel E Goldberg
1Howard Hughes Medical Institute, Washington University School of Medicine, Departments of Molecular Microbiology and Medicine, 660 S. Euclid Ave., Box 8230, St. Louis, Missouri 63110, USA.
Abstract:
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.
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