Immunodiagnostic/protective role of cathepsin L cysteine proteinases secreted by Fasciola species

Abstract

Cathepsin L, a major cysteine proteinase secreted by the parasite plays a pivotal role in various aspects of its pathogenecity. The enzyme takes part in nutrient acquisition by catabolizing host proteins to absorbable peptides, facilitates the migration of the parasite through the host intestine and liver by cleaving interstitial matrix proteins such as fibronectin, laminin and native collagen and is implicated in the inactivation of host immune defenses by cleaving immunoglobulins. Recently, Cathepsin L has been shown to suppress Th1 immune response in infected laboratory animals making them susceptible to concurrent bacterial infections. Accordingly, the protease has been recognized as an important target at which parasite intervention strategies should be directed. Fluke Cathepsin L cysteine proteinases are also reported as sensitive and specific markers for the immunodiagnosis of fasciolosis in ruminants. Further, vaccination of laboratory or large animals with these proteases resulted in a significant reduction in fluke burden and/or fecundity.