The differential expression of multiple isoenzyme forms during stage conversion of Toxoplasma gondii: an adaptive developmental strategy.
The apicomplexan parasite Toxoplasma gondii has the ability to switch between a rapidly replicating tachyzoite and a slowly dividing encysted bradyzoite within its intermediate hosts such as humans or other warm-blooded vertebrates. It is likely that in vivo, the tachyzoites differentiate into encysted bradyzoites in response to the immune system attack during disease progression. As part of a developmental strategy and, in order to survive within infected hosts, T. gondii tachyzoites undergo profound metabolic and morphological changes by differentiating into encysted bradyzoites. Bradyzoites are characterised by their resistance to both the immune system and chemotherapy. The stimulus that triggers Toxoplasma encystation and the molecular mechanisms triggering the switch from tachyzoite to bradyzoite remain unknown. It is very important to elucidate these mechanisms since bradyzoites within tissue cysts are not only the source of infection transmitted from domestic animals to humans, but can also be converted into tachyzoites that are the cause of fatal toxoplasmic encephalitis in acquired immunodeficiency syndrome patients. In this review, I focus on recent efforts towards the characterisation of genes that encode several stage-specific isoenzymes. The picture emerging from these studies is that stage-specific expression of isoenyzmes having different biochemical properties accompanies the interconversion of tachyzoite into bradyzoite, and vice versa. It can be hypothesised that the difference found between these enzymatic activities may be instrumental in maintaining some major parasitic metabolisms such as glycolysis in pace with the stage-specific requirements of carbohydrate or polysaccharide biosynthesis.
Tomavo
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Equipe de Parasitologie Moléculaire, Centre National de la Recherche Scientifique UMR No. 8576, Université des Sciences et Technologies de Lille, 59655 Cedex, Villeneuve d'Ascq, France. stan.tomavo@univ-lille1.fr
D000818:Animals; D051607:CDP-Diacylglycerol-Inositol 3-Phosphatidyltransferase; D018507:Gene Expression Regulation, Developmental / Q000235:genetics; D015971:Gene Expression Regulation, Enzymologic / Q000235:genetics; D005956:Glucose-6-Phosphate Isomerase / Q000096:biosynthesis / Q000235:genetics; D006801:Humans; D007527:Isoenzymes / Q000096:biosynthesis / Q000235:genetics*; D007770:L-Lactate Dehydrogenase / Q000737:chemistry / Q000235:genetics; D010751:Phosphopyruvate Hydratase / Q000096:biosynthesis / Q000235:genetics; D014122:Toxoplasma / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development*; D017855:Transferases (Other Substituted Phosphate Groups) / Q000096:biosynthesis / Q000235:genetics
D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase; D017855:Transferases (Other Substituted Phosphate Groups); D051607:CDP-Diacylglycerol-Inositol 3-Phosphatidyltransferase; D010751:Phosphopyruvate Hydratase; D005956:Glucose-6-Phosphate Isomerase