{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T05:14:11Z","timestamp":1790745251624,"version":"4.1.0"},"update-to":[{"DOI":"10.1371\/journal.ppat.1011867","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2023,12,21]],"date-time":"2023-12-21T00:00:00Z","timestamp":1703116800000}}],"reference-count":66,"publisher":"Public Library of Science (PLoS)","issue":"12","license":[{"start":{"date-parts":[[2023,12,11]],"date-time":"2023-12-11T00:00:00Z","timestamp":1702252800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000265","name":"Medical Research Council","doi-asserted-by":"publisher","award":["MR\/W002221\/1"],"award-info":[{"award-number":["MR\/W002221\/1"]}],"id":[{"id":"10.13039\/501100000265","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000265","name":"Medical Research Council","doi-asserted-by":"publisher","award":["MR\/W002221\/1"],"award-info":[{"award-number":["MR\/W002221\/1"]}],"id":[{"id":"10.13039\/501100000265","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100010269","name":"Wellcome Trust","doi-asserted-by":"publisher","award":["UNS85804"],"award-info":[{"award-number":["UNS85804"]}],"id":[{"id":"10.13039\/100010269","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100010269","name":"Wellcome Trust","doi-asserted-by":"publisher","award":["221681\/Z\/20\/Z"],"award-info":[{"award-number":["221681\/Z\/20\/Z"]}],"id":[{"id":"10.13039\/100010269","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p>\n                    The mitochondrial electron transport chain (mETC) is a series of membrane embedded enzymatic complexes critical for energy conversion and mitochondrial metabolism. In commonly studied eukaryotes, including humans and animals, complex II, also known as succinate dehydrogenase (SDH), is an essential four-subunit enzyme that acts as an entry point to the mETC, by harvesting electrons from the TCA cycle. Apicomplexa are pathogenic parasites with significant impact on human and animal health. The phylum includes\n                    <jats:italic>Toxoplasma gondii<\/jats:italic>\n                    which can cause fatal infections in immunocompromised people. Most apicomplexans, including\n                    <jats:italic>Toxoplasma<\/jats:italic>\n                    , rely on their mETC for survival, yet SDH remains largely understudied. Previous studies pointed to a divergent apicomplexan SDH with nine subunits proposed for the\n                    <jats:italic>Toxoplasma<\/jats:italic>\n                    complex, compared to four in humans. While two of the nine are homologs of the well-studied SDHA and B, the other seven have no homologs in SDHs of other systems. Moreover, SDHC and D, that anchor SDH to the membrane and participate in substrate bindings, have no homologs in Apicomplexa. Here, we validated five of the seven proposed subunits as bona fide SDH components and demonstrated their importance for SDH assembly and activity. We further find that all five subunits are important for parasite growth, and that disruption of SDH impairs mitochondrial respiration and results in spontaneous initiation of differentiation into bradyzoites. Finally, we provide evidence that the five subunits are membrane bound, consistent with their potential role in membrane anchoring, and we demonstrate that a DY motif in one of them, SDH10, is essential for complex formation and function. Our study confirms the divergent composition of\n                    <jats:italic>Toxoplasma<\/jats:italic>\n                    SDH compared to human, and starts exploring the role of the lineage-specific subunits in SDH function, paving the way for future mechanistic studies.\n                  <\/jats:p>","DOI":"10.1371\/journal.ppat.1011867","type":"journal-article","created":{"date-parts":[[2023,12,11]],"date-time":"2023-12-11T13:33:36Z","timestamp":1702301616000},"page":"e1011867","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":22,"title":["Functional and biochemical characterization of the Toxoplasma gondii succinate dehydrogenase complex"],"prefix":"10.1371","volume":"19","author":[{"given":"Mariana F.","family":"Silva","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kiera","family":"Douglas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sofia","family":"Sandalli","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9274-9486","authenticated-orcid":true,"given":"Andrew E.","family":"Maclean","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5909-2307","authenticated-orcid":true,"given":"Lilach","family":"Sheiner","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2023,12,11]]},"reference":[{"key":"ppat.1011867.ref001","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1016\/S0005-2728(01)00229-8","article-title":"The Saccharomyces cerevisiae mitochondrial succinate:ubiquinone oxidoreductase","volume":"1553","author":"BD Lemire","year":"2002","journal-title":"Biochim Biophys Acta"},{"key":"ppat.1011867.ref002","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1016\/j.mito.2010.03.001","article-title":"Succinate dehydrogenase\u2014Assembly, regulation and role in human disease","volume":"10","author":"J Rutter","year":"2010","journal-title":"Mitochondrion"},{"key":"ppat.1011867.ref003","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1080\/13510002.2020.1752002","article-title":"Mitochondrial complex II and reactive oxygen species in disease and therapy","volume":"25","author":"K Hadrava Vanova","year":"2020","journal-title":"Redox Rep"},{"key":"ppat.1011867.ref004","doi-asserted-by":"crossref","first-page":"7255","DOI":"10.1074\/jbc.M806623200","article-title":"Novel mitochondrial complex II isolated from Trypanosoma cruzi is composed of 12 peptides including a heterodimeric Ip subunit","volume":"284","author":"J Morales","year":"2009","journal-title":"J Biol Chem"},{"key":"ppat.1011867.ref005","doi-asserted-by":"crossref","first-page":"934","DOI":"10.1038\/s41586-023-05817-y","article-title":"Structural basis of mitochondrial membrane bending by the I-II-III2-IV2 supercomplex","volume":"615","author":"A M\u00fchleip","year":"2023","journal-title":"Nature"},{"key":"ppat.1011867.ref006","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1104\/pp.103.024620","article-title":"New insights into the respiratory chain of plant mitochondria. Supercomplexes and a unique composition of complex II","volume":"133","author":"H Eubel","year":"2003","journal-title":"Plant Physiol"},{"key":"ppat.1011867.ref007","doi-asserted-by":"crossref","first-page":"2542","DOI":"10.1038\/s41467-023-38158-5","article-title":"Structures of Tetrahymena thermophila respiratory megacomplexes on the tubular mitochondrial cristae.","volume":"14","author":"F Han","year":"2023","journal-title":"Nat Commun."},{"key":"ppat.1011867.ref008","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1126\/science.abn7747","article-title":"Structures of Tetrahymena\u2019s respiratory chain reveal the diversity of eukaryotic core metabolism","volume":"376","author":"L Zhou","year":"2022","journal-title":"Science"},{"key":"ppat.1011867.ref009","first-page":"7","author":"D Huet","year":"2018","journal-title":"Identification of cryptic subunits from an apicomplexan ATP 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