ArticleBMC microbiology2013
Enzymatically active Rho and Rac small-GTPases are involved in the establishment of the vacuolar membrane after Toxoplasma gondii invasion of host cells.
Article in BMC microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 23 citations in OpenAlex.
- Differential transcriptome study on the damage of testicular tissues caused by chronic infection of T. gondii in mice.Parasites & vectors · 2024Article
- Role of Host Small GTPases in Apicomplexan Parasite Infection.Microorganisms · 2022Review
- The type three secretion system effector protein IpgB1 promotes Shigella flexneri cell-to-cell spread through double-membrane vacuole escape.PLoS pathogens · 2022Article
- Article
- Effects of host vimentin on Eimeria tenella sporozoite invasion.Parasites & vectors · 2022Article
- Article
- Characterization of the erythrocyte GTPase Rac1 in relation to Plasmodium falciparum invasion.Scientific reports · 2020Article
- The Activin Receptor, Activin-Like Kinase 4, MediatesFrontiers in cellular and infection microbiology · 2019Article
- Genome-Wide CRISPR Screen Identifies Host Factors Required byFrontiers in cellular and infection microbiology · 2019Article
- MAP1203 PromotesFrontiers in cellular and infection microbiology · 2018Article
- Genome-Wide Bimolecular Fluorescence Complementation-Based Proteomic Analysis ofFrontiers in immunology · 2018Article
- Phosphoproteome ofThe American journal of tropical medicine and hygiene · 2017Article
- Subverting Host Cell P21-Activated Kinase: A Case of Convergent Evolution across Pathogens.Pathogens (Basel, Switzerland) · 2017Review
- Coevolution of RAC Small GTPases and their Regulators GEF Proteins.Evolutionary bioinformatics online · 2016Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
backgroundGTPases are the family of hydrolases that bind and hydrolyze guanosine triphosphate. The large Immunity-related GTPases and the small GTPase ADP-ribosylation factor-6 in host cells are known to accumulate on the parasitophorous vacuole membrane (PVM) of Toxoplasma gondii and play critical roles in this parasite infection, but these GTPases cannot explain the full extent of infection.
resultsIn this research, RhoA and Rac1 GTPases from the host cell were found to accumulate on the PVM regardless of the virulence of the T. gondii strains after T. gondii invasion, and this accumulation was dependent on their GTPase activity. The real-time micrography of T. gondii tachyzoites invading COS-7 cells overexpressing CFP-RhoA showed that this GTPase was recruited to the PVM at the very beginning of the invasion through the host cell membrane or from the cytosol. Host cell RhoA and Rac1 were also activated after T. gondii tachyzoites invasion, which was needed for host cell cytoskeleton reorganization to facilitate intracellular pathogens invasion. The decisive domains for the RhoA accumulation on the PVM included the GTP/Mg2+ binding site, the mDia effector interaction site, the G1 box, the G2 box and the G5 box, respectively, which were related to the binding of GTP for enzymatic activity and mDia for the regulation of microtubules. The recruited CFP-RhoA on the PVM could not be activated by epithelial growth factor (EGF) and no translocation was observed, unlike the unassociated RhoA in the host cell cytosol that migrated to the cell membrane towards the EGF activation spot. This result supported the hypothesis that the recruited RhoA or Rac1 on the PVM were in the GTP-bound active form. Wild-type RhoA or Rac1 overexpressed cells had almost the same infection rates by T. gondii as the mock-treated cells, while RhoA-N19 or Rac1-N17 transfected cells and RhoA, Rac1 or RhoA + Rac1 siRNA-treated cells showed significantly diminished infection rates compared to mock cells.
conclusionsThe accumulation of the RhoA and Rac1 on the PVM and the requisite of their normal GTPase activity for efficient invasion implied their involvement and function in T. gondii invasion.
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