ArticlePLoS neglected tropical diseases2023
Molecular characterization of a novel serine proteinase from Trichinella spiralis and its participation in larval invasion of gut epithelium.
Article in PLoS neglected tropical diseases, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 14 citations in OpenAlex.
- Trichinella spiralis galectin disrupts gut epithelial integrity and mediates larval invasion via acting MUC13- ROCK2/MAPK pathway.PLoS neglected tropical diseases · 2026Article
- Vaccination of mice with Trichinella spiralis serine proteinase enhanced gut epithelial barrier and elicited a high protective immunity.PLoS neglected tropical diseases · 2026Article
- Trichinella spiralis serine proteinase enhances antibody-dependent cell-mediated (ADCC) killing of newborn larvae by driving M1 polarization via the NF-κB pathway.Parasite (Paris, France) · 2026Article
- A Trichinella spiralis Trypsin Drives Macrophage M1 Polarization and Strengthens Cytotoxicity Killing Larvae via Activating the NF-κB Pathway.Transboundary and emerging diseases · 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
- Trichinella spiralis excretory-secretory proteins induced autophagy via activating AMPK/mTOR pathway and protected gut epithelial barrier.PLoS neglected tropical diseases · 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
- A Trichinella spiralis serine protease triggers gut epithelial apoptosis and destroys the barrier integrity to mediate larval invasion.PLoS neglected tropical diseases · 2025Article
- Molecular characterization of zinc metalloproteinase Nas-14 from Trichinella spiralis and its participation in intestinal invasion.PLoS neglected tropical diseases · 2025Article
- Effects of Trichinella spiralis and its serine protease inhibitors on intestinal mucosal barrier function.Veterinary research · 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
- Trichinella spiralis excretory/secretory proteins mediated larval invasion via inducing gut epithelial apoptosis and barrier disruption.PLoS neglected tropical diseases · 2025Article
- A NovelInternational journal of molecular sciences · 2024Article
- Biological characteristics of a new long-chain fatty acid transport protein 1 from Trichinella spiralis and its participation in lipid metabolism, larval moulting, and development.Veterinary research · 2024Article
- Enhanced Genomic and Transcriptomic Resources forInternational journal of molecular sciences · 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
- Biological characteristics and functions of a novel glutamate dehydrogenase from Trichinella spiralis.Parasite (Paris, France) · 2024Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundA novel serine proteinase of Trichinells spiralis (TsSPc) has been identified in the excretion/secretion (ES) antigens, but its role in larval invasion is unclear. The aim of this study was to clone and express TsSPc, identify its biological and biochemical characteristics, and investigate its role on larval invasion of gut epithelium during T. spiralis infection. METHODOLOGY/PRINCIPAL
findingsTsSPc has a functional domain of serine proteinase, and its tertiary structure consists of three amino acid residues (His88, Asp139 and Ser229) forming a pocket like functional domain. Recombinant TsSPc (rTsSPc) was expressed and purified. The rTsSPc has good immunogenicity. On Western blot analysis, rTsSPc was recognized by infection serum and anti-rTsSPc serum, natural TsSPc in crude and ES antigens was identified by anti-rTsSPc serum. The results of qPCR, Western blot and indirect immunofluorescence test (IIFT) showed that TsSPc was expressed at diverse stage worms, and mainly localized at cuticle, stichosome and intrauterine embryos of this nematode. The rTsSPc had enzymatic activity of native serine protease, which hydrolyzed the substrate BAEE, casein and collagen I. After site directed mutation of enzymatic active sites of TsSPc, its antigenicity did not change but the enzyme activity was fully lost. rTsSPc specifically bound to intestinal epithelium cells (IECs) and the binding sites were mainly localized in cell membrane and cytoplasm. rTsSPc accelerated larval invasion of IECs, whereas anti-rTsSPc antibodies and TsSPc-specific dsRNA obviously hindered larval invasion.
conclusionsTsSPc was a surface and secretory proteinase of the parasite, participated in larval invasion of gut epithelium, and may be considered as a candidate vaccine target molecule against Trichinella intrusion and infection.
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