ArticleScientific reports2016
Characterization of aspartyl aminopeptidase from Toxoplasma gondii.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 26 citations in OpenAlex.
- A Major Facilitator Superfamily Transporter Is Critical for the Metabolism and Biogenesis of the Apicoplast.Pathogens (Basel, Switzerland) · 2025Article
- A novel YGGT family protein is localized in the apicoplast and is essential for the organelle inheritance.Frontiers in cellular and infection microbiology · 2025Article
- Apicoplast biogenesis mediated by ATG8 requires the ATG12-ATG5-ATG16L and SNAP29 complexes inAutophagy · 2023Article
- An unconventional SNARE complex mediates exocytosis at the plasma membrane and vesicular fusion at the apical annuli in Toxoplasma gondii.PLoS pathogens · 2023Article
- Article
- RecombinantVaccines · 2021Article
- Localization and enzyme kinetics of aminopeptidase N3 from Toxoplasma gondii.Parasitology research · 2020Article
- The Biochemical and Functional Characterization of M28 Aminopeptidase Protein Secreted byMolecules (Basel, Switzerland) · 2019Article
- Characterization of metalloproteases and serine proteases of Toxoplasma gondii tachyzoites and their effect on epithelial cells.Parasitology research · 2019Article
- Metallopeptidases of Toxoplasma gondii: in silico identification and gene expression.Parasite (Paris, France) · 2018Article
- Biochemical characterization of aminopeptidase N2 from Toxoplasma gondii.The Journal of veterinary medical science · 2017Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aminopeptidases have emerged as new promising drug targets for the development of novel anti-parasitic drugs. An aspartyl aminopeptidase-like gene has been identified in the Toxoplasma gondii genome (TgAAP), although its function remains unknown. In this study, we characterized TgAAP and performed functional analysis of the gene product. Firstly, we expressed a functional recombinant TgAAP (rTgAAP) protein in Escherichia coli, and found that it required metal ions for activity and showed a substrate preference for N-terminal acidic amino acids Glu and Asp. Then, we evaluated the function and drug target potential of TgAAP using the CRISPR/Cas9 knockout system. Western blotting demonstrated the deletion of TgAAP in the knockout strain. Indirect immunofluorescence analysis showed that TgAAP was localized in the cytoplasm of the wild-type parasite, but was not expressed in the knockout strain. Phenotype analysis revealed that TgAAP knockout inhibited the attachment/invasion, replication, and substrate-specific activity in T. gondii. Finally, the activity of drug CID 23724194, previously described as targeting Plasmodium and malarial parasite AAP, was tested against rTgAAP and the parasite. Overall, TgAAP knockout affected the growth of T. gondii but did not completely abolish parasite replication and growth. Therefore, TgAAP may comprise a useful adjunct drug target of T. gondii.
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Registered trials
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