ArticleMolecular and biochemical parasitology2009
The cathepsin L of Toxoplasma gondii (TgCPL) and its endogenous macromolecular inhibitor, toxostatin.
Article in Molecular and biochemical parasitology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 47 citations in OpenAlex.
- Insights into Octopus maya cathepsins from metatranscriptome and genome: structure evolutionary relationships and functional role prediction in digestive processes.Biology open · 2025Article
- Purification and characterization of cysteine protease of Sarcocystis fusiformis from infected Egyptian water buffaloes.Scientific reports · 2023Article
- The Toxoplasma plant-like vacuolar compartment (PLVAC).The Journal of eukaryotic microbiology · 2022Review
- The Dually Localized EF-Hand Domain-Containing Protein TgEFP1 Regulates the Lytic Cycle ofCells · 2022Article
- Discovery and Optimization of Triazine Nitrile Inhibitors ofACS chemical neuroscience · 2020Article
- Cysteine proteases in protozoan parasites.PLoS neglected tropical diseases · 2018Review
- Article
- A Perspective on Thiazolidinone Scaffold Development as a New Therapeutic Strategy for Toxoplasmosis.Frontiers in cellular and infection microbiology · 2018Article
- Screen of Non-annotated Small Secreted Proteins of Pseudomonas syringae Reveals a Virulence Factor That Inhibits Tomato Immune Proteases.PLoS pathogens · 2016Article
- Microbial inhibitors of cysteine proteases.Medical microbiology and immunology · 2016Review
- Identification and characterization of a cathepsin-L-like peptidase in Eimeria tenella.Parasitology research · 2014Article
- Localization of eimeripain, an Eimeria tenella cathepsin B-like cysteine protease, during asexual and sexual intracellular development in chicken ceca.The Journal of veterinary medical science · 2014Article
- Inhibitor of cysteine proteases is critical for motility and infectivity of Plasmodium sporozoites.mBio · 2013Article
- Toxoplasma gondii cathepsin proteases are undeveloped prominent vaccine antigens against toxoplasmosis.BMC infectious diseases · 2013Article
- Cysteine protease inhibitor (AcStefin) is required for complete cyst formation of Acanthamoeba.Eukaryotic cell · 2013Article
- Cathepsin proteases in Toxoplasma gondii.Advances in experimental medicine and biology · 2011Review
- Cathepsin L occupies a vacuolar compartment and is a protein maturase within the endo/exocytic system of Toxoplasma gondii.Molecular microbiology · 2010Article
- Characterization of a novel organelle in Toxoplasma gondii with similar composition and function to the plant vacuole.Molecular microbiology · 2010Article
- Exoerythrocytic Plasmodium parasites secrete a cysteine protease inhibitor involved in sporozoite invasion and capable of blocking cell death of host hepatocytes.PLoS pathogens · 2010Article
- Toxoplasma gondii cathepsin L is the primary target of the invasion-inhibitory compound morpholinurea-leucyl-homophenyl-vinyl sulfone phenyl.The Journal of biological chemistry · 2009Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Toxoplasma gondii is an obligate intracellular parasite of all vertebrates, including man. Successful invasion and replication requires the synchronized release of parasite proteins, many of which require proteolytic processing. Unlike most parasites, T. gondii has a limited number of Clan CA, family C1 cysteine proteinases with one cathepsin B (TgCPB), one cathepsin L (TgCPL) and three cathepsin Cs (TgCPC1, 2, 3). Previously, we characterized toxopain, the only cathepsin B enzyme, which localizes to the rhoptry organelle. Two cathepsin Cs are trafficked through dense granules to the parasitophorous vacuole where they degrade peptides. We now report the cloning, expression, and modeling of the sole cathepsin L gene and the identification of two new endogenous inhibitors. TgCPL differs from human cathepsin L with a pH optimum of 6.5 and its substrate preference for leucine (vs. phenylalanine) in the P2 position. This distinct preference is explained by homology modeling, which reveals a non-canonical aspartic acid (Asp 216) at the base of the predicted active site S2 pocket, which limits substrate access. To further our understanding of the regulation of cathepsins in T. gondii, we identified two genes encoding endogenous cysteine proteinase inhibitors (ICPs or toxostatins), which are active against both TgCPB and TgCPL in the nanomolar range. Over expression of toxostatin-1 significantly decreased overall cysteine proteinase activity in parasite lysates, but had no detectable effect on invasion or intracellular multiplication. These findings provide important insights into the proteolytic cascades of T. gondii and their endogenous control.
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