ArticleThe Korean journal of parasitology2018
Molecular and Biochemical Properties of a Cysteine Protease of Acanthamoeba castellanii.
Article in The Korean journal of parasitology, 2018. 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, 19 citations in OpenAlex.
- Acanthamoeba castellanii cysteine protease 3 promotes M1 macrophage polarization through the TLR4/NF‑κB pathway.Parasites & vectors · 2025Article
- Unraveling the interplay between unicellular parasites and bacterial biofilms: Implications for disease persistence and antibiotic resistance.Virulence · 2024Review
- Staurosporine as a Potential Treatment forMarine drugs · 2024Article
- Epidemiology of and Genetic Factors Associated withPathogens (Basel, Switzerland) · 2024Review
- Induction of Programmed Cell Death inAntioxidants (Basel, Switzerland) · 2023Article
- Biological characteristics and pathogenicity ofFrontiers in microbiology · 2023Review
- Trogocytosis in Unicellular Eukaryotes.Cells · 2021Review
- Identification and biochemical characterisation of Acanthamoeba castellanii cysteine protease 3.Parasites & vectors · 2020Article
- Insight into the Lifestyle of AmoebaMicroorganisms · 2020Article
- Paradigms of Protist/Bacteria Symbioses Affecting Human Health:Frontiers in microbiology · 2020Review
- Review
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
Abstract
Acanthamoeba spp. are free-living protozoa that are opportunistic pathogens for humans. Cysteine proteases of Acanthamoeba have been partially characterized, but their biochemical and functional properties are not clearly understood yet. In this study, we isolated a gene encoding cysteine protease of A. castellanii (AcCP) and its biochemical and functional properties were analyzed. Sequence analysis of AcCP suggests that this enzyme is a typical cathepsin L family cysteine protease, which shares similar structural characteristics with other cathepsin L-like enzymes. The recombinant AcCP showed enzymatic activity in acidic conditions with an optimum at pH 4.0. The recombinant enzyme effectively hydrolyzed human proteins including hemoglobin, albumin, immunoglobuins A and G, and fibronectin at acidic pH. AcCP mainly localized in lysosomal compartment and its expression was observed in both trophozoites and cysts. AcCP was also identified in cultured medium of A. castellanii. Considering to lysosomal localization, secretion or release by trophozoites and continuous expression in trophozoites and cysts, the enzyme could be a multifunctional enzyme that plays important biological functions for nutrition, development and pathogenicity of A. castellanii. These results also imply that AcCP can be a promising target for development of chemotherapeutic drug for Acanthamoeba infections.
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Registered trials
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