Submitted to: Molecular and Biochemical Parasitology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 6/19/1998
Publication Date: N/A
Citation: N/A Interpretive Summary: Trichuris suis in swine causes severe clinical disease in moderate to heavy infections. Symptoms include mucohemorhagic diarrhea, anemia weight loss, anorexia, and death, usually in young animals. Much of the pathology in T. suis infection is associated with the tissue penetration activities of the larvae and adult parasites. We have identified an enzyme from excretory/secretory products of adult worms which appears to be involved in burrowing and feeding of the parasite. This enzyme was cloned from a cDNA library of adult T. suis, and its molecular sequence was determined. The enzyme may represent an attractive target for control strategies aimed at this parasite.
Technical Abstract: We have used oligonucleotide primers corresponding to the enzyme active site and the highly conserved nematode splice leader sequence (SL1) to clone the full length sequence of a Trichuris suis metalloprotease cDNA (TS 6-18). The cDNA sequence contained an open reading frame of 1274 bp. Transformation of the DH5a cell line with the pGEX-3 plasmid expression vector and subsequent induction of synthesis of a glutathione s-transferase-fusion protein (GST-TS 6-18) in the transformants with IPTG produced a 72 kDa protein which reacted strongly with a rabbit polyclonal antibody produced against the previously characterized native 45kDa protein.