ArticleNature communications2021
Structural insights into an atypical secretory pathway kinase crucial for Toxoplasma gondii invasion.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Functional dissection of prenyltransferases reveals roles in endocytosis and secretory vacuolar sorting in type 2-ME49 strain ofVirulence · 2024Article
- An inhibitory segment within G-patch activators tunes Prp43-ATPase activity during ribosome assembly.Nature communications · 2024Article
- Eimeria: Navigating complex intestinal ecosystems.PLoS pathogens · 2024Review
- Article
- Proteomic approaches for protein kinase substrate identification in Apicomplexa.Molecular and biochemical parasitology · 2024Review
- Toxoplasma gondii rhoptry discharge factor 3 is essential for invasion and microtubule-associated vesicle biogenesis.PLoS biology · 2024Article
- Sustained rhoptry docking and discharge requires Toxoplasma gondii intraconoidal microtubule-associated proteins.Nature communications · 2024Article
- The emerging role ofFrontiers in immunology · 2024Review
- Conoid extrusion regulates glideosome assembly to control motility and invasion in Apicomplexa.Nature microbiology · 2022Article
- Temporal and thermal profiling of theeLife · 2022Article
- Ceramide biosynthesis is critical for establishment of the intracellular niche of Toxoplasma gondii.Cell reports · 2022Article
- Paving the Way: Contributions of Big Data to Apicomplexan and Kinetoplastid Research.Frontiers in cellular and infection microbiology · 2022Review
Corrections and comments
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Authors and funding
13 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Active host cell invasion by the obligate intracellular apicomplexan parasites relies on the formation of a moving junction, which connects parasite and host cell plasma membranes during entry. Invading Toxoplasma gondii tachyzoites secrete their rhoptry content and insert a complex of RON proteins on the cytoplasmic side of the host cell membrane providing an anchor to which the parasite tethers. Here we show that a rhoptry-resident kinase RON13 is a key virulence factor that plays a crucial role in host cell entry. Cryo-EM, kinase assays, phosphoproteomics and cellular analyses reveal that RON13 is a secretory pathway kinase of atypical structure that phosphorylates rhoptry proteins including the components of the RON complex. Ultimately, RON13 kinase activity controls host cell invasion by anchoring the moving junction at the parasite-host cell interface.
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