Molecular characterization of a novel serine proteinase from Trichinella spiralis and its participation in larval invasion of gut epithelium.

ABSTRACT:

Background

A 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 findings

TsSPc 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 Ts

SUBMITTER: Song YY 

PROVIDER: S-EPMC10513378 | biostudies-literature | 2023 Sep

REPOSITORIES: biostudies-literature