ArticleCell chemical biology2021
Toxoplasma gondii serine hydrolases regulate parasite lipid mobilization during growth and replication within the host.
Article in Cell chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 9 citations in OpenAlex.
- A Spinster-like Transporter at the Inner Membrane Complex is critical for Toxoplasma gondii cytokinesis, motility and invasion.PLoS pathogens · 2026Article
- A key role of PIEZO2 mechanosensitive ion channel in adipose sensory innervation.Cell metabolism · 2025Article
- Reference Gene Selection for RT-qPCR Normalization inInternational journal of molecular sciences · 2024Article
- Mixed alkyl/aryl phosphonates identify metabolic serine hydrolases as antimalarial targets.Cell chemical biology · 2024Article
- The intersection of hostMicrobiology and molecular biology reviews : MMBR · 2024Review
- Lipid metabolism: the potential targets for toxoplasmosis treatment.Parasites & vectors · 2024Review
- Mixed Alkyl/Aryl Phosphonates Identify Metabolic Serine Hydrolases as Antimalarial Targets.bioRxiv : the preprint server for biology · 2024Article
- Article
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
Abstract
The intracellular protozoan parasite Toxoplasma gondii must scavenge cholesterol and other lipids from the host to facilitate intracellular growth and replication. Enzymes responsible for neutral lipid synthesis have been identified but there is no evidence for enzymes that catalyze lipolysis of cholesterol esters and esterified lipids. Here, we characterize several T. gondii serine hydrolases with esterase and thioesterase activities that were previously thought to be depalmitoylating enzymes. We find they do not cleave palmitoyl thiol esters but rather hydrolyze short-chain lipid esters. Deletion of one of the hydrolases results in alterations in levels of multiple lipids species. We also identify small-molecule inhibitors of these hydrolases and show that treatment of parasites results in phenotypic defects reminiscent of parasites exposed to excess cholesterol or oleic acid. Together, these data characterize enzymes necessary for processing lipids critical for infection and highlight the potential for targeting parasite hydrolases for therapeutic applications.
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