Journal
NATURE METHODS
Volume 4, Issue 12, Pages 1007-1009Publisher
NATURE RESEARCH
DOI: 10.1038/nmeth1132
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- NIAID NIH HHS [AI47798] Funding Source: Medline
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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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