Publications by authors named "Yang Xiu Yue Xu"
Article Synopsis
- Trichinella spiralis is a dangerous foodborne parasite, and developing a vaccine targeting it is crucial for ensuring meat safety in food animals.
- The study focused on a protein called Tsgal found on the parasite, which was used to create a vaccine using Lactobacillus plantarum to elicit immune responses in mice.
- Results showed that the vaccine successfully triggered specific immune responses and significantly reduced the number of adult worms in the intestines of vaccinated mice, showcasing its potential as a protective measure against Trichinella infections.
Background: Trichinellosis is a serious zoonotic disease distributed around the world. It is needed to develop a safe, effective and feasible anti-Trichinella vaccine for prevention and control of trichinellosis. The aim of this study was to construct a recombinant Lactobacillus plantarum encoding Trichinella spiralis inorganic pyrophosphatase (TsPPase) and investigate its immune protective effects against T.
View Article and Find Full Text PDFInorganic pyrophosphatase (PPase) participates in energy cycle and plays a vital role in hydrolysis of inorganic pyrophosphate (PPi) into inorganic phosphate (Pi). The aim of this study was to investigate the biological properties of a Trichinella spiralis PPase (TsPPase) and its role in larval molting and developmental process. The predicted TsPPase consisted of 367 amino acids with a molecular mass of 41.
View Article and Find Full Text PDFThe aim of this study was to characterize the biological properties of a novel aspartic protease-1 from Trichinella spiralis (TsASP1) and evaluate its potential in inducing immune response. TsASP1 gene was cloned and expressed in Escherichia coli BL21 (DE3). On Western blotting analysis with anti-rTsASP1 serum, native TsASP1 was detected in various T.
View Article and Find Full Text PDFArticle Synopsis
- - The study focused on characterizing T. spiralis aspartic protease-2 (TsASP2) and its role in the invasion of intestinal epithelial cells (IECs) using RNA interference (RNAi) techniques.
- - Recombinant TsASP2 was shown to cleave various host proteins and displayed host-specific proteolytic activity, primarily affecting mouse hemoglobin, while its activity was significantly inhibited by the compound pepstatin A.
- - The findings revealed that TsASP2 promotes larval invasion of IECs, and when TsASP2 expression was suppressed using siRNA, larval invasion was inhibited, leading to reduced adult worm burden and fecundity in infected mice.