ArticleMolecular biology of the cell2006
A cleavable propeptide influences Toxoplasma infection by facilitating the trafficking and secretion of the TgMIC2-M2AP invasion complex.
Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
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67 citing papers in PubMed.
- TGIF is a Golgin-like protein required for Golgi structural maintenance and function inbioRxiv : the preprint server for biology · 2026Article
- Tepsin and AP4 mediate transport from the trans-Golgi to the plant-like vacuole in toxoplasma.The Journal of cell biology · 2025Article
- Kinase function of TgTKL1 is essential for its role inmSphere · 2024Article
- Functional Characterization of 11 Tentative Microneme Proteins in Type I RH Strain ofAnimals : an open access journal from MDPI · 2024Article
- A conserved complex of microneme proteins mediates rhoptry discharge in Toxoplasma.The EMBO journal · 2023Article
- Article
- Functional screening revealsmBio · 2023Article
- Structural insights into MIC2 recognition by MIC2-associated protein in Toxoplasma gondii.Communications biology · 2023Article
- Metallic Nanoparticles and Core-Shell Nanosystems in the Treatment, Diagnosis, and Prevention of Parasitic Diseases.Pathogens (Basel, Switzerland) · 2023Review
- A cathepsin C-like protease post-translationally modifiesbioRxiv : the preprint server for biology · 2023Article
- Regulation of phosphoinositide metabolism in Apicomplexan parasites.Frontiers in cell and developmental biology · 2023Review
- An image-based high-content screening for compounds targetingFrontiers in cellular and infection microbiology · 2023Article
- Effects of different drugs and hormone treatment on Toxoplasma gondii glutathione S-transferase 2.Parasites & vectors · 2022Article
- The Toxoplasma plant-like vacuolar compartment (PLVAC).The Journal of eukaryotic microbiology · 2022Review
- Do All Coccidia Follow the Same Trafficking Rules?Life (Basel, Switzerland) · 2021Review
- Emerging Mechanisms of Endocytosis inLife (Basel, Switzerland) · 2021Review
- Article
- A highly dynamic F-actin network regulates transport and recycling of micronemes in Toxoplasma gondii vacuoles.Nature communications · 2019Article
- The Toxoplasma Vacuolar HCell reports · 2019Article
- Article
7 more citing papers are in PubMed but not listed here.
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6 authors.
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Abstract
Propeptides regulate protein function and trafficking in many eukaryotic systems and have emerged as important features of regulated secretory proteins in parasites of the phylum Apicomplexa. Regulated protein secretion from micronemes and host cell invasion are inextricably linked and essential processes for the apicomplexan parasite Toxoplasma gondii. TgM2AP is a propeptide-containing microneme protein found in a heterohexameric complex with the microneme protein TgMIC2, a protein that has a demonstrated fundamental role in gliding motility and invasion. TgM2AP function is also central to these processes, because disruption of TgM2AP (m2apKO) results in secretory retention of TgMIC2, leading to reduced TgMIC2 secretion from the micronemes and impaired invasion. Because the TgM2AP propeptide is predicted to be processed in an intracellular site near where TgMIC2 is retained in m2apKO parasites, we hypothesized that the propeptide and its proteolytic removal influence trafficking and secretion of the complex. We found that proTgM2AP traffics through endosomal compartments and that deletion of the propeptide leads to defective trafficking of the complex within or near this site, resulting in aberrant processing and decreased secretion of TgMIC2, impaired invasion, and reduced virulence in vivo, mirroring the phenotypes observed in m2apKO parasites. In contrast, mutation of several cleavage site residues resulted in normal localization, but it affected the stability and secretion of the complex from the micronemes. Therefore, the propeptide and its cleavage site influence distinct aspects of TgMIC2-M2AP function, with both impacting the outcome of infection.
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