ArticleVeterinary research2022
Molecular characterization and determination of the biochemical properties of cathepsin L of Trichinella spiralis.
Article in Veterinary research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 19 citations in OpenAlex.
- Vaccination of mice with Trichinella spiralis serine proteinase enhanced gut epithelial barrier and elicited a high protective immunity.PLoS neglected tropical diseases · 2026Article
- Melanin Metabolism: A Novel Oxidative Degradation Mechanism and Regulation by Hydrolyzed Conchiolin Protein.Journal of cosmetic dermatology · 2026Article
- Catalytically Active Recombinant Cysteine Proteases ofInternational journal of molecular sciences · 2025Article
- Trichinella spiralis serine protease mediates larval invasion of gut epithelium via binding to CK8 and activating RhoA/ROCK1 pathway.PLoS neglected tropical diseases · 2025Article
- Staphyloxanthin loaded niosomal nanocarrier augments its anthelmintic activity against Trichinella spiralis infection in mice.Scientific reports · 2025Article
- Vaccination of mice with Trichinella spiralis C-type lectin elicited the protective immunity and enhanced gut epithelial barrier function.PLoS neglected tropical diseases · 2025Article
- Silencing Ditylenchus destructor cathepsin L-like cysteine protease has negative pleiotropic effect on nematode ontogenesis.Scientific reports · 2024Article
- A novel trypsin of Trichinella spiralis mediates larval invasion of gut epithelium via binding to PAR2 and activating ERK1/2 pathway.PLoS neglected tropical diseases · 2024Article
- A novel Trichinella spiralis serine proteinase disrupted gut epithelial barrier and mediated larval invasion through binding to RACK1 and activating MAPK/ERK1/2 pathway.PLoS neglected tropical diseases · 2024Article
- Trichinella spiralis cathepsin L damages the tight junctions of intestinal epithelial cells and mediates larval invasion.PLoS neglected tropical diseases · 2023Article
- Trichinella spiralis cathepsin L induces macrophage M1 polarization via the NF-κB pathway and enhances the ADCC killing of newborn larvae.Parasites & vectors · 2023Article
- Binding of Trichinella spiralis C-type lectin with syndecan-1 on intestinal epithelial cells mediates larval invasion of intestinal epithelium.Veterinary research · 2023Article
- Molecular characterization of a novel serine proteinase from Trichinella spiralis and its participation in larval invasion of gut epithelium.PLoS neglected tropical diseases · 2023Article
- A candidate subunit vaccine induces protective immunity against Mycobacterium avium subspecies paratuberculosis in mice.NPJ vaccines · 2023Article
- Identification and genetic characterisatin of cathepsin L in Demodex.Experimental & applied acarology · 2023Article
- Tandem mass tag-based quantitative proteomics analyses of a chicken-original virulent and its attenuatedFrontiers in veterinary science · 2023Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Cathepsin L is an important cysteine protease, but its function in T. spiralis remains unclear. The aim of this research was to explore the biological characteristics of T. spiralis cathepsin L (TsCatL) and its role in T. spiralis-host interactions. Bioinformatic analysis revealed the presence of the cysteine protease active site residues Gln, Cys, His and Asn in mature TsCatL, as well as specific motifs of cathepsin L similar to ERFNIN and GYLND in the prepeptide of TsCatL. Molecular docking of mature TsCatL and E64 revealed hydrophobic effects and hydrogen bonding interactions. Two domains of TsCatL (TsCatL2) were cloned and expressed, and recombinant TsCatL2 (rTsCatL2) was autocatalytically cleaved under acidic conditions to form mature TsCatL. TsCatL was transcribed and expressed in larvae and adults and located in the stichosome, gut and embryo. Enzyme kinetic tests showed that rTsCatL2 degraded the substrate Z-Phe-Arg-AMC under acidic conditions, which was inhibited by E64 and PMSF and enhanced by EDTA, L-cysteine and DTT. The kinetic parameters of rTsCatL2 were a Km value of 48.82 μM and Vmax of 374.4 nM/min at pH 4.5, 37 °C and 5 mM DTT. In addition, it was shown that rTsCatL2 degraded haemoglobin, serum albumin, immunoglobulins (mouse IgG, human IgG and IgM) and extracellular matrix components (fibronectin, collagen I and laminin). The proteolytic activity of rTsCatL2 was host specific and significantly inhibited by E64. rTsCatL2 possesses the natural activity of a sulfhydryl-containing cysteine protease, and TsCatL is an important digestive enzyme that seems to be important for the nutrient acquisition, immune evasion and invasion of Trichinella in the host.
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