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• W4386142858 abstract "Artemisinin (ART) resistance in Plasmodium is threatening the artemisinin combination therapies (ACTs)- the first line of defense against malaria. ART resistance has been established to be mediated by the Plasmodium Kelch13 (PfK13) protein. For the crucial role of PfK13 in multiple pathways of Plasmodium life cycle and ART resistance, it becomes imperative to investigate its interacting partners. We recombinantly expressed PfK13-p (BTB/POZ & propeller domains), generated anti-PfK13-p antibodies to perform coimmunoprecipitation (co-IP) assays to probe PfK13 interacting partners. Suface plasmon resonance (SPR) and pull-down assays were performed to establish physical interactions of representative proteins with PfK13-p. The co-IP assays identified 17 proteins with distinct functions in the parasite life cycle- protein folding, cellular metabolism and protein binding & invasion. In addition to the overlap with previously identified proteins, our study identified 10 unique proteins. Fructose-biphosphate aldolase (FBA) and heat shock protein 70 (HSP70) demonstrated strong biophysical interaction with PfK13-p with KD values 6.6 µM and 7.6 µM, respectively. Additionally, PfMSP1 formed a complex with PfK13-p which is evident from the pull-down assay. This study adds to our knowledge of PfK13 protein in mediating ART resistance by identifying new PfK13-interacting partners. Three representative proteins- fructose-biphosphate aldolase (FBA), heat shock protein 70 (HSP70) and merozoite surface protein 1 (MSP1) demonstrated clear evidence of biophysical interactions with PfK13-p. However, elucidation of the functional relevance of these physical interactions are crucial in context of PfK13 role in ART resistance." @default.
• W4386142858 created "2023-08-25" @default.
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• W4386142858 date "2023-12-01" @default.
• W4386142858 modified "2023-09-29" @default.
• W4386142858 title "Artemisinin resistance in P. falciparum: Probing the interacting partners of Kelch13 protein in parasite" @default.
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• W4386142858 doi "https://doi.org/10.1016/j.jgar.2023.08.012" @default.
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