Molecular & Cellular Proteomics· 2026Q1
Thermal proteome profiling identifies new drug targets in Plasmodium falciparum parasites
- 2citations
- Q1SCImago
- 2026year
Short summary
A novel proteome-wide cellular thermal shift assay pipeline, including a membrane solubilization step, identified new drug targets in Plasmodium falciparum parasites, validating ACS10 for MMV665915 and mapping parasite responses to atovaquone and cipargamin.
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Key points
- Screened 25 antimalarials against Plasmodium falciparum using proteome-wide CETSA and molecular docking.
- Validated ACS10 as the target for the antimalarial MMV665915.
- Discovered new, previously unknown drug targets in P. falciparum.
- Updated the CETSA pipeline with a membrane solubilization step for improved analysis.
- Validated targets for atovaquone and cipargamin in both cell lysates and intact cells.
AI-generated from the title and abstract; the full text is not read.
Abstract
Spreading resistance to clinically used antimalarial drugs increases the need for identification of new drug targets. Here, we screened 25 antimalarials with known and unknown mode of action to validate old and find new drug targets in P. falciparum. Combining experimental approach by proteome-wide cellular thermal shift assay and computational filtering by molecular docking, we found the drugs to bind to previously known drug targets, validated ACS10 as the target of MMV665915 and discovered new drug targets. Furthermore, we updated the experimental and analytical MS-CETSA pipeline with the inclusion of membrane solubilization step, validated the targets of atovaquone and cipargamin on cell lysates and in intact cells and mapped the parasite response to these antimalarials.
The authors' abstract, as published at the source. Molecular & Cellular Proteomics, 2026 · DOI ↗
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Field: Public Health, Environmental and Occupational Health
Public Health, Environmental and Occupational HealthMedicine