ArticleThe Korean journal of parasitology2019
Partial Characterization of Two Cathepsin D Family Aspartic Peptidases of Clonorchis sinensis.
Article in The Korean journal of parasitology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 10 citations in OpenAlex.
- Crystal structure of Schistosoma mansoni cathepsin D1 in complex with a nanobody reveals the conformation of the propeptide-bound state.Acta crystallographica. Section D, Structural biology · 2026Article
- Molecular characterization of a novel Trichinella spiralis aspartyl protease and its role in the larval invasion of host intestinal epithelial cells.Parasite (Paris, France) · 2026Article
- Clonorchis sinensis excretory/secretory proteins ameliorate inflammation in rheumatoid arthritis and ankylosing spondylitis.Parasites & vectors · 2025Article
- Article
- pH-Dependent Structural Dynamics of Cathepsin D-Family Aspartic Peptidase ofPathogens (Basel, Switzerland) · 2021Article
- Dopaminergic antagonists inhibit bile chemotaxis of adult Clonorchis sinensis and its egg production.PLoS neglected tropical diseases · 2020Article
- Identification and Analysis of the Tegument Protein and Excretory-Secretory Products of the Carcinogenic Liver FlukeFrontiers in microbiology · 2020Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Cathepsin D (CatD, EC 3.4.23.5) is a member belonging to the subfamily of aspartic endopeptidases, which are classified into the MEROPS clan AA, family A1. Helminth parasites express a large set of different peptidases that play pivotal roles in parasite biology and pathophysiology. However, CatD is less well known than the other classes of peptidases in terms of biochemical properties and biological functions. In this study, we identified 2 novel CatDs (CsCatD1 and CsCatD2) of Clonorchis sinensis and partially characterized their properties. Both CsCatDs represent typical enzymes sharing amino acid residues and motifs that are tightly conserved in the CatD superfamily of proteins. Both CsCatDs showed similar patterns of expression in different developmental stages of C. sinensis, but CsCatD2 was also expressed in metacercariae. CsCatD2 was mainly expressed in the intestines and eggs of C. sinensis. Sera obtained from rats experimentally infected with C. sinensis reacted with recombinant CsCatD2 beginning 2 weeks after infection and the antibody titers were gradually increased by maturation of the parasite. Structural analysis of CsCatD2 revealed a bilobed enzyme structure consisting of 2 antiparallel β-sheet domains packed against each other forming a homodimeric structure. These results suggested a plausible biological role of CsCatD2 in the nutrition and reproduction of parasite and its potential utility as a serodiagnostic antigen in clonorchiasis.
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