ArticleScientific reports2021
Identifying the major lactate transporter of Toxoplasma gondii tachyzoites.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 28 citations in OpenAlex.
- Article
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- A two-membrane gateway for monocarboxylates couples host glycolysis tobioRxiv : the preprint server for biology · 2026Article
- Transporters, an important but poorly studied area of Toxoplasma gondii.Parasites & vectors · 2026Review
- Impact of Iron Overload and Hypomagnesemia Combination on Pediatric Allogeneic Hematopoietic Stem Cell Transplantation Outcomes.Nutrients · 2025Article
- paraCell: a novel software tool for the interactive analysis and visualization of standard and dual host-parasite single-cell RNA-seq data.Nucleic acids research · 2025Article
- Metabolic changes inmBio · 2024Article
- Microbial membrane transport proteins and their biotechnological applications.World journal of microbiology & biotechnology · 2024Review
- Metabolic changes to host cells withbioRxiv : the preprint server for biology · 2023Article
- Temporal and thermal profiling of theeLife · 2022Article
- Systematic identification of the lysine lactylation in the protozoan parasite Toxoplasma gondii.Parasites & vectors · 2022Article
- Toxoplasma gondii excretion of glycolytic products is associated with acidification of the parasitophorous vacuole during parasite egress.PLoS pathogens · 2022Article
- Real-Time Analysis of Mitochondrial Electron Transport Chain Function inBio-protocol · 2022Article
- A single amino acid exchange converts FocA into a unidirectional efflux channel for formate.Microbiology (Reading, England) · 2022Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Toxoplasma gondii and Plasmodium falciparum parasites both extrude L-lactate, a byproduct of glycolysis. The P. falciparum Formate Nitrite Transporter, PfFNT, mediates L-lactate transport across the plasma membrane of P. falciparum parasites and has been validated as a drug target. The T. gondii genome encodes three FNTs that have been shown to transport L-lactate, and which are proposed to be the targets of several inhibitors of T. gondii proliferation. Here, we show that each of the TgFNTs localize to the T. gondii plasma membrane and are capable of transporting L-lactate across it, with TgFNT1 making the primary contribution to L-lactate transport during the disease-causing lytic cycle of the parasite. We use the Xenopus oocyte expression system to provide direct measurements of L-lactate transport via TgFNT1. We undertake a genetic analysis of the importance of the tgfnt genes for parasite proliferation, and demonstrate that all three tgfnt genes can be disrupted individually and together without affecting the lytic cycle under in vitro culture conditions. Together, our experiments identify the major lactate transporter in the disease causing stage of T. gondii, and reveal that this transporter is not required for parasite proliferation, indicating that TgFNTs are unlikely to be targets for anti-Toxoplasma drugs.
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