ArticleParasites & vectors2018
Characterization of a serine protease inhibitor from Trichinella spiralis and its participation in larval invasion of host's intestinal epithelial cells.
Article in Parasites & vectors, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 72 citations in OpenAlex.
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- Heterologous expression and functional characterization of recombinant arenin to assess its anticancer and wound-healing potential.Bioresources and bioprocessing · 2025Article
- 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
- 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
- Galactomannan inhibits Trichinella spiralis invasion of intestinal epithelium cells and enhances antibody-dependent cellular cytotoxicity related killing of larvae by driving macrophage polarization.Parasite (Paris, France) · 2024Article
- Trichinella spiralis galectin binding to toll-like receptor 4 induces intestinal inflammation and mediates larval invasion of gut mucosa.Veterinary research · 2023Article
- Effects ofInfection and immunity · 2023Article
- Identification of antigens in the Trichinella spiralis extracellular vesicles for serological detection of early stage infection in swine.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
- Trichinella spiralis dipeptidyl peptidase 1 suppressed macrophage cytotoxicity by promoting M2 polarization via the STAT6/PPARγ pathway.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
- The gut microbiota contributes to changes in the host immune response induced by Trichinella spiralis.PLoS neglected tropical diseases · 2023Article
- A novel C-type lectin from Trichinella spiralis mediates larval invasion of host intestinal epithelial cells.Veterinary research · 2022Article
- 3D Biofabrication of a Cardiac Tissue Construct for Sustained Longevity and Function.ACS applied materials & interfaces · 2022Article
- Proteases secreted by Trichinella spiralis intestinal infective larvae damage the junctions of the intestinal epithelial cell monolayer and mediate larval invasion.Veterinary research · 2022Article
- Regulatory effects of Trichinella spiralis and a serine protease inhibitor on the endoplasmic reticulum stress response of intestinal epithelial cells.Veterinary research · 2022Article
- Serine protease inhibitor derived fromFrontiers in cellular and infection microbiology · 2022Article
- Characterization of a novel cysteine protease in Trichinella spiralis and its role in larval intrusion, development and fecundity.Veterinary research · 2021Article
- Proteomics of Gnathostomiasis: A Way Forward for Diagnosis and Treatment Development.Pathogens (Basel, Switzerland) · 2021Review
- Adjuvanticity of β -Glucan for Vaccine AgainstFrontiers in cell and developmental biology · 2021Article
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
backgroundTrichinella spiralis serine protease inhibitor (TsSPI) was identified in ES proteins of adult worms (AW), the TsSPI gene was highly expressed at enteral stage worms (AW and newborn larvae), distributed mainly in the cuticle and stichosome of this nematode. Vaccination of mice with rTsSPI exhibited a 62.2% reduction of intestinal AW and a 57.25% reduction of muscle larvae after larval challenge. The aim of this study was to investigate the biological characteristics of TsSPI and its roles in the process of T. spiralis invasion of host's intestinal epithelium cells (IECs).
methodsThe rTsSPI inhibition on trypsin enzymatic activity was detected by SDS-PAGE and spectrophotometry. The binding of rTsSPI with intestinal epithelium from normal mice and the primary cultured mouse intestinal epithelium cells (IECs) was examined by indirect immunofluorescent (IIF), the cellular localization of rTsSPI binding to IECs was observed by confocal microscopy. The inhibition of anti-rTsSPI serum on T. spiralis invasion of IECs was determined by an in vitro invasion assay. Anti-rTsSPI antibody cytotoxicity on the newborn larvae (NBL) was also determined.
resultsThe rTsSPI had the inhibitory activity against porcine trypsin. The rTsSPI specifically bound to the intestinal epithelium from normal mice and primary cultured mouse IECs, and the binding sites were located in IEC membrane and cytoplasm. Anti-rTsSPI antibodies depressed the larval invasion of IECs with a dose-dependent mode. Anti-rTsSPI antibodies also participated in the destruction of T. spiralis NBL via an ADCC-mediated manner.
conclusionsTsSPI might participate in the T. spiralis larval invasion of IECs and it is likely the potential vaccine target against T. spiralis enteral stages.
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