ArticleThe Journal of biological chemistry2013
Functional dissection of Toxoplasma gondii perforin-like protein 1 reveals a dual domain mode of membrane binding for cytolysis and parasite egress.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Molecular mechanism of pore formation by Plasmodium Perforin-like Protein 2.Nature communications · 2026Article
- Article
- An in vivo fitness gene of Toxoplasma, MIC11, is essential for PLP1-mediated egress from host cells.Nature communications · 2026Article
- Article
- The invasion pore induced by Toxoplasma gondii.EMBO reports · 2025Article
- Evaluation ofRecent advances in inflammation & allergy drug discovery · 2025Article
- Article
- Egress Regulatory Factors: HowPathogens (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 apical membrane complex for triggering rhoptry exocytosis and invasion in Toxoplasma.The EMBO journal · 2022Article
- Temporal and thermal profiling of theeLife · 2022Article
- Life cycle stages, specific organelles and invasion mechanisms ofParasitology · 2020Review
- Perforin-Like Proteins of Apicomplexan Parasites.Frontiers in cellular and infection microbiology · 2020Review
- An apically located hybrid guanylate cyclase-ATPase is critical for the initiation of CaThe Journal of biological chemistry · 2019Article
- Structural basis of Toxoplasma gondii perforin-like protein 1 membrane interaction and activity during egress.PLoS pathogens · 2018Article
- Pathways of host cell exit by intracellular pathogens.Microbial cell (Graz, Austria) · 2018Review
- Protein kinase A negatively regulates Ca2+ signalling in Toxoplasma gondii.PLoS biology · 2018Article
- Structural Basis of Phosphatidic Acid Sensing by APH in Apicomplexan Parasites.Structure (London, England : 1993) · 2018Article
- Structures of monomeric and oligomeric forms of theScience advances · 2018Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The recently discovered role of a perforin-like protein (PLP1) for rapid host cell egress by the protozoan parasite Toxoplasma gondii expanded the functional diversity of pore-forming proteins. Whereas PLP1 was found to be necessary for rapid egress and pathogenesis, the sufficiency for and mechanism of membrane attack were yet unknown. Here we further dissected the PLP1 knock-out phenotype, the mechanism of PLP1 pore formation, and the role of each domain by genetic complementation. We found that PLP1 is sufficient for membrane disruption and has a conserved mechanism of pore formation through target membrane binding and oligomerization to form large, multimeric membrane-embedded complexes. The highly conserved, central MACPF domain and the β-sheet-rich C-terminal domain were required for activity. Loss of the unique N-terminal extension reduced lytic activity and led to a delay in rapid egress, but did not significantly decrease virulence, suggesting that small amounts of lytic activity are sufficient for pathogenesis. We found that both N- and C-terminal domains have membrane binding activity, with the C-terminal domain being critical for function. This dual mode of membrane association may promote PLP1 activity and parasite egress in the diverse cell types in which this parasite replicates.
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