Proteomics

Dataset Information

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FKBP35 secures ribosome homeostasis in Plasmodium falciparum


ABSTRACT: Plasmodium falciparum accounts for the majority of over 600’000 malaria-associated deaths annually. Parasites resistant to nearly all antimalarials have emerged and the need for drugs with alternative modes of action is thus undoubted. The FK506-binding protein PfFKBP35 has gained attention as a promising drug target due to its high affinity to the macrolide compound FK506. Whilst there is considerable interest in targeting PfFKBP35 with small molecules, a genetic validation of this factor as a drug target is missing and its function in parasite biology remains elusive. Here, we show that limiting PfFKBP35 levels are lethal to P. falciparum and result in a delayed-death phenotype that is characterized by defective ribosome homeostasis and protein translation. We furthermore show that the drug exerts it parasiticidal activity in a PfFKBP35-independent manner and, using cellular thermal shift assays, identify FK506-targets beyond PfFKBP35. In addition to revealing first insights on PfFKBP35 function, our results show that current efforts to develop PfFKBP35-targeting drugs need to be reconsidered.

INSTRUMENT(S): Orbitrap Eclipse

ORGANISM(S): Plasmodium Falciparum

SUBMITTER: Katarzyna Buczak  

LAB HEAD: Alexander Schmidt

PROVIDER: PXD039018 | Pride | 2023-10-18

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
001_BT-001_G22.raw Raw
002_BT-001_G22.raw Raw
003_BT-001_G22.raw Raw
004_BT-001_G22.raw Raw
005_BT-001_G22.raw Raw
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