ArticleScientific reports2017
Mitochondrial behaviour throughout the lytic cycle of Toxoplasma gondii.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 90 citations in OpenAlex.
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- A novel targeting domain directs essential components of the cytosolic iron-sulfur cluster assembly pathway to the mitochondrion of Toxoplasma parasites.PLoS biology · 2025Article
- Structure, assembly and inhibition of the Toxoplasma gondii respiratory chain supercomplex.Nature structural & molecular biology · 2025Article
- Proline dehydrogenase, a rate-limiting catabolic enzyme, affecting the growth and pathogenicity of Toxoplasma gondii tachyzoites by regulating the proline metabolism and mitochondrial function of the parasite.Parasites & vectors · 2025Article
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- Phosphatase UBLCP1 is required for the growth, virulence and mitochondrial integrity of Toxoplasma gondii.Parasites & vectors · 2025Article
- The dynamin-related protein PfDyn2 is essential for both apicoplast and mitochondrial fission inmBio · 2025Article
- Myosin A and F-Actin play a critical role in mitochondrial dynamics and inheritance in Toxoplasma gondii.PLoS pathogens · 2024Article
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- Two ancient membrane pores mediate mitochondrial-nucleus membrane contact sites.The Journal of cell biology · 2024Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Mitochondria distribution in cells controls cellular physiology in health and disease. Here we describe the mitochondrial morphology and positioning found in the different stages of the lytic cycle of the eukaryotic single-cell parasite Toxoplasma gondii. The lytic cycle, driven by the tachyzoite life stage, is responsible for acute toxoplasmosis. It is known that whilst inside a host cell the tachyzoite maintains its single mitochondrion at its periphery. We found that upon parasite transition from the host cell to the extracellular matrix, mitochondrion morphology radically changes, resulting in a reduction in peripheral proximity. This change is reversible upon return to the host, indicating that an active mechanism maintains the peripheral positioning found in the intracellular stages. Comparison between the two states by electron microscopy identified regions of coupling between the mitochondrion outer membrane and the parasite pellicle, whose features suggest the presence of membrane contact sites, and whose abundance changes during the transition between intra- and extra-cellular states. These novel observations pave the way for future research to identify molecular mechanisms involved in mitochondrial distribution in Toxoplasma and the consequences of these mitochondrion changes on parasite physiology.
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