{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T10:47:26Z","timestamp":1789555646889,"version":"build-2803163510"},"reference-count":50,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2015,4,11]],"date-time":"2015-04-11T00:00:00Z","timestamp":1428710400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2015,6]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>The intracellular parasite <jats:styled-content style=\"fixed-case\"><jats:italic>T<\/jats:italic><\/jats:styled-content><jats:italic>oxoplasma gondii<\/jats:italic> converts from a rapidly replicating tachyzoite form during acute infection to a quiescent encysted bradyzoite stage that persists inside long\u2010lived cells during chronic infection. Bradyzoites adopt reduced metabolism and slow replication while waiting for an opportunity to recrudesce the infection within the host. Interconversion between these two developmental stages is characterized by expression of glycolytic isoenzymes that play key roles in parasite metabolism. The parasite genome encodes two isoforms of lactate dehydrogenase (<jats:styled-content style=\"fixed-case\">LDH1<\/jats:styled-content> and <jats:styled-content style=\"fixed-case\">LDH2<\/jats:styled-content>) and enolase (<jats:styled-content style=\"fixed-case\">ENO1<\/jats:styled-content> and <jats:styled-content style=\"fixed-case\">ENO2<\/jats:styled-content>) that are expressed in a stage\u2010specific manner. Expression of different isoforms of these enzymes allows <jats:styled-content style=\"fixed-case\"><jats:italic>T<\/jats:italic><\/jats:styled-content><jats:italic>. gondii<\/jats:italic> to rapidly adapt to diverse metabolic requirements necessary for either a rapid replication of the tachyzoite stage or a quiescent lifestyle typical of the bradyzoites. Herein we identified unspliced forms of <jats:styled-content style=\"fixed-case\">LDH<\/jats:styled-content> and <jats:styled-content style=\"fixed-case\">ENO<\/jats:styled-content> transcripts produced during transition between these two parasite stages suggestive of an intron retention mechanism to promptly exchange glycolytic isoforms for rapid adaptation to environmental changes. We also identified key regulatory elements in the <jats:styled-content style=\"fixed-case\">ENO<\/jats:styled-content> transcription units, revealing cooperation between the <jats:styled-content style=\"fixed-case\">ENO2<\/jats:styled-content> 5\u2032\u2010untranslated region and the <jats:styled-content style=\"fixed-case\">ENO2<\/jats:styled-content> intron, along with identifying a role for the <jats:styled-content style=\"fixed-case\">ENO1<\/jats:styled-content> 3\u2032\u2010untranslated region in stage\u2010specific expression.<\/jats:p>","DOI":"10.1111\/mmi.12999","type":"journal-article","created":{"date-parts":[[2015,3,16]],"date-time":"2015-03-16T11:34:39Z","timestamp":1426505679000},"page":"1159-1175","source":"Crossref","is-referenced-by-count":31,"title":["Expression of the glycolytic enzymes enolase and lactate dehydrogenase during the early phase of <scp><i>T<\/i><\/scp><i>oxoplasma<\/i> differentiation is regulated by an intron retention mechanism"],"prefix":"10.1111","volume":"96","author":[{"given":"Matteo","family":"Lunghi","sequence":"first","affiliation":[{"name":"Department of Chemistry, Biology and Biotechnology University of Perugia  Perugia Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3134-7480","authenticated-orcid":false,"given":"Roberto","family":"Galizi","sequence":"additional","affiliation":[{"name":"Department of Experimental Medicine University of Perugia  Perugia Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alessandro","family":"Magini","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Biology and Biotechnology University of Perugia  Perugia Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vern B.","family":"Carruthers","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology University of Michigan Medical School  Ann Arbor MI 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