<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Zeng JM</submitter><funding>Australian Research Council</funding><pagination>6787</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC7991638</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>11(1)</volume><pubmed_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-lacta</pubmed_abstract><journal>Scientific reports</journal><pubmed_title>Identifying the major lactate transporter of Toxoplasma gondii tachyzoites.</pubmed_title><pmcid>PMC7991638</pmcid><funding_grant_id>DP200100483</funding_grant_id><funding_grant_id>Discovery Projects DP150102883</funding_grant_id><funding_grant_id>Discovery Early Career Researcher Award DE160101035</funding_grant_id><funding_grant_id>Future Fellowship 1053082</funding_grant_id><pubmed_authors>Lehane AM</pubmed_authors><pubmed_authors>Martin RE</pubmed_authors><pubmed_authors>Hapuarachchi SV</pubmed_authors><pubmed_authors>Shafik SH</pubmed_authors><pubmed_authors>Zeng JM</pubmed_authors><pubmed_authors>van Dooren GG</pubmed_authors><pubmed_authors>Kirk K</pubmed_authors></additional><is_claimable>false</is_claimable><name>Identifying the major lactate transporter of Toxoplasma gondii tachyzoites.</name><description>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-lacta</description><dates><release>2021-01-01T00:00:00Z</release><publication>2021 Mar</publication><modification>2025-04-05T15:25:07.272Z</modification><creation>2025-04-05T15:25:07.272Z</creation></dates><accession>S-EPMC7991638</accession><cross_references><pubmed>33762657</pubmed><doi>10.1038/s41598-021-86204-3</doi></cross_references></HashMap>