Helminth glutathione peroxidase (GPx)

Helminth glutathione peroxidase (GPx) is a vital antioxidant enzyme utilized by parasitic worms to neutralize reactive oxygen species (ROS) encountered within the host environment. During infection, host immune cells such as neutrophils and macrophages release ROS, including hydrogen peroxide and lipid hydroperoxides, as a primary defense mechanism to eliminate the parasite. Helminth GPx enzymes, which are frequently secreted or localized to the parasite's surface tegument, catalyze the reduction of these harmful oxidants into non-toxic water or alcohols using glutathione as a reducing agent (Cookson et al., 1992; Mei & LoVerde, 1997). This enzymatic activity is essential for maintaining the integrity of the parasite's cellular membranes and preventing oxidative damage to its DNA, thereby facilitating long-term survival and chronic infection (Sayed & Williams, 2004). Because of its critical role in parasite survival and its accessibility as a secreted protein, helminth GPx is considered a high-priority target for the development of novel anthelmintic drugs and vaccine strategies. Inhibiting this enzyme increases the parasite's susceptibility to host-mediated oxidative stress, potentially leading to the clearance of the infection (Sies, 1993).

Other names

Parasite glutathione peroxidaseSecreted glutathione peroxidasePhospholipid hydroperoxide glutathione peroxidase-like proteinGPx-1GPx-2

Inhibition of the enzyme's catalytic activity, preventing the reduction of hydroperoxides and leading to the accumulation of reactive oxygen species and oxidative damage within the parasite.