ArticlePLoS neglected tropical diseases2023
Trichinella spiralis cathepsin L damages the tight junctions of intestinal epithelial cells and mediates larval invasion.
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 6 papers.
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Who cites it
6 citing papers in PubMed, 6 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
- 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 serine protease triggers gut epithelial apoptosis and destroys the barrier integrity to mediate larval invasion.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
- 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
- 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
backgroundCathepsin L, a lysosomal enzyme, participates in diverse physiological processes. Recombinant Trichinella spiralis cathepsin L domains (rTsCatL2) exhibited natural cysteine protease activity and hydrolyzed host immunoglobulin and extracellular matrix proteins in vitro, but its functions in larval invasion are unknown. The aim of this study was to explore its functions in T. spiralis invasion of the host's intestinal epithelial cells. METHODOLOGY/PRINCIPAL
findingsRNAi significantly suppressed the expression of TsCatL mRNA and protein with TsCatL specific siRNA-302. T. spiralis larval invasion of Caco-2 cells was reduced by 39.87% and 38.36%, respectively, when anti-TsCatL2 serum and siRNA-302 were used. Mice challenged with siRNA-302-treated muscle larvae (ML) exhibited a substantial reduction in intestinal infective larvae, adult worm, and ML burden compared to the PBS group, with reductions of 44.37%, 47.57%, and 57.06%, respectively. The development and fecundity of the females from the mice infected with siRNA-302-treated ML was significantly inhibited. After incubation of rTsCatL2 with Caco-2 cells, immunofluorescence test showed that the rTsCatL2 gradually entered into the cells, altered the localization of cellular tight junction proteins (claudin 1, occludin and zo-1), adhesion junction protein (e-cadherin) and extracellular matrix protein (laminin), and intercellular junctions were lost. Western blot showed a 58.65% reduction in claudin 1 expression in Caco-2 cells treated with rTsCatL2. Co-IP showed that rTsCatL2 interacted with laminin and collagen I but not with claudin 1, e-cadherin, occludin and fibronectin in Caco-2 cells. Moreover, rTsCatL2 disrupted the intestinal epithelial barrier by inducing cellular autophagy.
conclusionsrTsCatL2 disrupts the intestinal epithelial barrier and facilitates T. spiralis larval invasion.
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