Publications by authors named "Chen Le Li"
Background: Cathepsin 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.
View Article and Find Full Text PDFBackground: During the early stages of Trichinella spiralis infection, macrophages predominantly undergo polarization to the M1-like phenotype, causing the host's inflammatory response and resistance against T. spiralis infection. As the disease progresses, the number of M2-type macrophages gradually increases, contributing to tissue repair processes within the host.
View Article and Find Full Text PDFArticle Synopsis
- TsCatL, a cysteine protease from T. spiralis, was studied to understand its biological role and function in interactions with the host.
- Bioinformatics indicated crucial active site residues and specific motifs associated with proteolytic activity, while molecular studies showed that TsCatL could cleave various substrates, including proteins important for the host's immune response.
- The enzyme demonstrated significant activity under acidic conditions, with its function being crucial for T. spiralis's nutrient acquisition and evasion of the host's immune system.