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Acyl-CoA synthetase 10 (Plasmodium falciparum) (PfACS10)

Target: PfACS10
Molecular classification: Enzyme, Acyl-CoA synthetase family

Overview

Acyl-CoA synthetase 10 (PfACS10) is an essential enzyme in *Plasmodium falciparum* that activates free fatty acids for use in lipid biosynthesis, especially triglycerides[1][2][5][9]. Conditional knockdown and genetic studies demonstrate that PfACS10 is required for parasite growth in the asexual blood stage[1][2][3]. Small-molecule inhibitors of PfACS10 are lethal to the parasite, validating it as a drug target for malaria therapy[1][2][3][7][10]. Drug resistance emerges through specific point mutations in PfACS10, which offers both a challenge and a biomarker for patient monitoring and efficacy assessment[1][2][7]. MMV1582367 (GSK701), a PfACS10 inhibitor, has advanced to phase I clinical trials for uncomplicated malaria[2].

Other names: PfACS10acyl-CoA synthetase 10 (Plasmodium falciparum)PF3D7_0525100

Mechanism of action

Inhibitors block PfACS10's acyl-CoA formation activity, impairing lipid biosynthesis and causing parasite death by disrupting triglyceride formation and altering fatty acid profiles

Biological functions

Lipid metabolism (activation of free fatty acids for biosynthetic processes)Triglyceride biosynthesis

Disease associations

Infection (malaria)

Safety considerations

Potential for drug resistance due to mutations in PfACS10 (e.g., lining the fatty acid binding pocket)Need for selectivity to avoid off-target effects, given conservation of acyl-CoA synthetases across species

Interacting drugs

MMV665924

3 more in the full profile.

Biomarkers

Mutations such as M300I, A268D/V, F427L in PfACS10 can be used to monitor drug resistance and susceptibility

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