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Structural insights into an atypical secretory pathway kinase crucial for Toxoplasma gondii invasion
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Structural insights into an atypical secretory pathway kinase crucial for Toxoplasma gondii invasion
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Journal Article
Structural insights into an atypical secretory pathway kinase crucial for Toxoplasma gondii invasion
2021
Overview
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.
Host cell invasion by
Toxoplasma gondii
depends on the heavily phosphorylated RON complex, but the relevance and regulation of these modifications are not understood. Here, the authors identify the kinase RON13 as a key virulence factor, determine its structure and show that it phosphorylates the RON complex.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
