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The parasite encodes diverse enzymes of glutathione and peroxide metabolism, but their physiological roles remain poorly understood. Herein, we shed a new perspective on the functions and relevance of the peroxiredoxin and glutathione metabolism in the zoonotic pathogen\n                    <jats:italic>T. gondii<\/jats:italic>\n                    . We show that two cytosolic peroxidases (\n                    <jats:italic>Tg<\/jats:italic>\n                    PRX1,\n                    <jats:italic>Tg<\/jats:italic>\n                    PRX2), a mitochondrial peroxiredoxin (\n                    <jats:italic>Tg<\/jats:italic>\n                    PRX3), and the cytosolic glutathione reductase (\n                    <jats:italic>Tg<\/jats:italic>\n                    GR2), glutamate\u2010cysteine ligase (\n                    <jats:italic>Tg<\/jats:italic>\n                    GCL), and glutathione synthetase (\n                    <jats:italic>Tg<\/jats:italic>\n                    GS) are not required for the lytic cycle of\n                    <jats:italic>T. gondii<\/jats:italic>\n                    under standard growth conditions. However, mutants lacking the gene for either\n                    <jats:italic>Tg<\/jats:italic>\n                    PRX1 or\n                    <jats:italic>Tg<\/jats:italic>\n                    GR2 exhibited increased susceptibility to exogenous hydrogen peroxide compared to wild\u2010type parasites. Furthermore, we found that the combined deletion of\n                    <jats:italic>Tg<\/jats:italic>\n                    PRX1 and\n                    <jats:italic>Tg<\/jats:italic>\n                    PRX2 led to a notable impairment of parasite growth, suggesting a functional redundancy between the two peroxidases. Finally, our results show that the apicoplast glutathione reductase (\n                    <jats:italic>Tg<\/jats:italic>\n                    GR1) is required for normal parasite growth in\u00a0vitro and in\u00a0vivo but is not essential for parasite survival. Our findings highlight that the redox metabolism of\n                    <jats:italic>Toxoplasma<\/jats:italic>\n                    is surprisingly robust and flexible, allowing the parasite to survive under the loss of several key enzymes of peroxide and glutathione metabolism.\n                  <\/jats:p>","DOI":"10.1096\/fj.202402341r","type":"journal-article","created":{"date-parts":[[2025,3,11]],"date-time":"2025-03-11T12:01:44Z","timestamp":1741694504000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["<i>Toxoplasma<\/i>\n                    survives the loss of key enzymes of peroxide and glutathione metabolism"],"prefix":"10.1096","volume":"39","author":[{"ORCID":"https:\/\/orcid.org\/0009-0006-3115-9278","authenticated-orcid":false,"given":"Qinghong","family":"Guo","sequence":"first","affiliation":[{"name":"State Key Laboratory for Animal Disease Control and Prevention, College of Veterinary Medicine South China Agricultural University  Guangzhou China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0003-2823-3375","authenticated-orcid":false,"given":"Jiajia","family":"Pan","sequence":"additional","affiliation":[{"name":"State Key Laboratory for Animal Disease Control and Prevention, College of Veterinary Medicine South China Agricultural University  Guangzhou China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0000-5654-8479","authenticated-orcid":false,"given":"Xuefang","family":"Guo","sequence":"additional","affiliation":[{"name":"State Key Laboratory for Animal Disease Control and Prevention, College of Veterinary Medicine South China Agricultural University  Guangzhou China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0006-1029-709X","authenticated-orcid":false,"given":"Meng","family":"Zhao","sequence":"additional","affiliation":[{"name":"State 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