Cloning, expression and characterisation of a cysteine protease from Trichinella spiralis.

Cysteine protease is a superfamily of widespread proteolytic enzymes and plays a major role in larval invasion, migration, exsheathing, survival and immune evasion in parasites. In the present study, the gene coding cysteine proteinase of the nematode Trichinella spiralis (Owen, 1835) was cloned into pQE-80L and subsequently expressed in E. coli JM109.

Characterization of a Trichinella spiralis putative serine protease. Study of its potential as sero-diagnostic tool.

Background: Trichinellosis is a serious zoonositc parasitosis worldwide. Because its clinical manifestations aren't specific, the diagnosis of trichinellosis is not easy to be made. Trichinella spiralis muscle larva (ML) excretory-secretory (ES) antigens are the most widely applied diagnostic antigens for human trichinellosis, but the major drawback of the ES antigens for assaying anti-Trichinella antibodies is the false negative in the early Trichinella infection period.

Characterization of a putative glutathione S-transferase of the parasitic nematode Trichinella spiralis.

The aim of this study was to identify the biological characteristics and functions of a putative Trichinella spiralis glutathione S-transferase (TspGST). The results of real-time PCR and immunofluorescent test (IFT) showed that the TspGST gene was expressed at all of T. spiralis different developmental stages (muscle larvae, intestinal infective larvae, adult worms and newborn larvae).

Cloning and expression of a Trichinella spiralis putative glutathione S-transferase and its elicited protective immunity against challenge infections.

Background: Glutathione-S-transferase (GST) is a widespread multigene family of detoxification enzymes. The vaccination of mice with recombinant GST of 24 kDa from Trichinella spiralis elicited a low immune protection against challenge infection. The objective of this study was to characterize the T.