{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T10:45:57Z","timestamp":1788345957704,"version":"build-2803163510"},"update-to":[{"DOI":"10.1371\/journal.ppat.1009835","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2021,9,7]],"date-time":"2021-09-07T00:00:00Z","timestamp":1630972800000}}],"reference-count":71,"publisher":"Public Library of Science (PLoS)","issue":"8","license":[{"start":{"date-parts":[[2021,8,25]],"date-time":"2021-08-25T00:00:00Z","timestamp":1629849600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000923","name":"australian research council","doi-asserted-by":"crossref","award":["DP150102883"],"award-info":[{"award-number":["DP150102883"]}],"id":[{"id":"10.13039\/501100000923","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100000923","name":"Australian Research Council","doi-asserted-by":"crossref","award":["DP200100483"],"award-info":[{"award-number":["DP200100483"]}],"id":[{"id":"10.13039\/501100000923","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100000925","name":"National Health and Medical Research Council","doi-asserted-by":"publisher","award":["APP1154540"],"award-info":[{"award-number":["APP1154540"]}],"id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p>\n                    Intracellular parasites of the phylum Apicomplexa are dependent on the scavenging of essential amino acids from their hosts. We previously identified a large family of apicomplexan-specific plasma membrane-localized amino acid transporters, the ApiATs, and showed that the\n                    <jats:italic>Toxoplasma gondii<\/jats:italic>\n                    transporter\n                    <jats:italic>Tg<\/jats:italic>\n                    ApiAT1 functions in the selective uptake of arginine.\n                    <jats:italic>Tg<\/jats:italic>\n                    ApiAT1 is essential for parasite virulence, but dispensable for parasite growth in medium containing high concentrations of arginine, indicating the presence of at least one other arginine transporter. Here we identify\n                    <jats:italic>Tg<\/jats:italic>\n                    ApiAT6-1 as the second arginine transporter. Using a combination of parasite assays and heterologous characterisation of\n                    <jats:italic>Tg<\/jats:italic>\n                    ApiAT6-1 in\n                    <jats:italic>Xenopus laevis<\/jats:italic>\n                    oocytes, we demonstrate that\n                    <jats:italic>Tg<\/jats:italic>\n                    ApiAT6-1 is a general cationic amino acid transporter that mediates both the high-affinity uptake of lysine and the low-affinity uptake of arginine.\n                    <jats:italic>Tg<\/jats:italic>\n                    ApiAT6-1 is the primary lysine transporter in the disease-causing tachyzoite stage of\n                    <jats:italic>T<\/jats:italic>\n                    .\n                    <jats:italic>gondii<\/jats:italic>\n                    and is essential for parasite proliferation. We demonstrate that the uptake of cationic amino acids by\n                    <jats:italic>Tg<\/jats:italic>\n                    ApiAT6-1 is \u2018\n                    <jats:italic>trans<\/jats:italic>\n                    -stimulated\u2019 by cationic and neutral amino acids and is likely promoted by an inwardly negative membrane potential. These findings demonstrate that\n                    <jats:italic>T<\/jats:italic>\n                    .\n                    <jats:italic>gondii<\/jats:italic>\n                    has evolved overlapping transport mechanisms for the uptake of essential cationic amino acids, and we draw together our findings into a comprehensive model that highlights the finely-tuned, regulated processes that mediate cationic amino acid scavenging by these intracellular parasites.\n                  <\/jats:p>","DOI":"10.1371\/journal.ppat.1009835","type":"journal-article","created":{"date-parts":[[2021,8,25]],"date-time":"2021-08-25T13:40:25Z","timestamp":1629898825000},"page":"e1009835","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":22,"title":["Coordinated action of multiple transporters in the acquisition of essential cationic amino acids by the intracellular parasite Toxoplasma gondii"],"prefix":"10.1371","volume":"17","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1530-7876","authenticated-orcid":true,"given":"Stephen 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J.","family":"McConville","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5613-2622","authenticated-orcid":true,"given":"Kiaran","family":"Kirk","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8040-1634","authenticated-orcid":true,"given":"Stefan","family":"Br\u00f6er","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2455-9821","authenticated-orcid":true,"given":"Giel G.","family":"van Dooren","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2021,8,25]]},"reference":[{"issue":"10","key":"ppat.1009835.ref001","doi-asserted-by":"crossref","first-page":"2448","DOI":"10.1128\/JCM.00487-16","article-title":"Laboratory Diagnosis of Congenital 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