ArticleParasitology research2014
Identification and characterization of the second cysteine protease inhibitor of Clonorchis sinensis (CsStefin-2).
Article in Parasitology research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 22 citations in OpenAlex.
- Inhibitor of Cysteine Protease ofPathogens (Basel, Switzerland) · 2022Article
- Fowlerstefin, a cysteine protease inhibitor of Naegleria fowleri, induces inflammatory responses in BV-2 microglial cells in vitro.Parasites & vectors · 2020Article
- Identification and Analysis of the Tegument Protein and Excretory-Secretory Products of the Carcinogenic Liver FlukeFrontiers in microbiology · 2020Article
- Article
- Cysteine proteases as digestive enzymes in parasitic helminths.PLoS neglected tropical diseases · 2018Review
- A novel type I cystatin of parasite origin with atypical legumain-binding domain.Scientific reports · 2017Article
- Inactivation of proteolytic enzymes by cestodes.Doklady biological sciences : proceedings of the Academy of Sciences of the USSR, Biological sciences sections · 2017Article
- Evolutionary analysis of the cystatin family in three Schistosoma species.Frontiers in genetics · 2014Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
CsStefin-2, the second cysteine protease inhibitor of Clonorchis sinensis, was identified and characterized. CsStefin-2 is a cysteine protease inhibitor that belongs to family 1 stefins based on its phylogenetic and structural properties. However, CsStefin-2 had a QIVSG cystatin motif distinct from the common QVVAG cystatin motif that is well conserved in family 1 stefins. Mutagenesis analysis revealed that the two amino acid substitutions in the QIVSG cystatin motif of CsStefin-2 did not affect its inhibitory activity. Molecular modeling also indicated that no critical change was induced in the interaction between CsStefin-2 and its target enzyme. CsStefin-2 showed broad inhibitory activities against several cysteine proteases, including human cathepsins B and L, papain, and cathepsin Fs of C. sinensis (CsCFs), and effectively inhibited the autocatalytic maturation of CsCF-6. Native CsStefin-2 was assembled into a homo-tetramer, in which intermolecular disulfide bonds are not involved in the assembly of the tetramer. CsStefin-2 was expressed throughout the various developmental stages of the parasite and was localized in the intestinal epithelium, where CsCFs are actively synthesized. These results suggest that CsStefin-2 is the second active cysteine protease inhibitor of C. sinensis that shares functional redundancy with CsStefin-1 to modulate the activity and processing of CsCFs.
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