Catalytically Active Recombinant Cysteine Proteases of <i>Haemonchus contortus:</i> Their Ability to Degrade Host Blood Proteins and Modulate Coagulation.

ABSTRACT: Haemonchus contortus is a blood-feeding gastrointestinal nematode that significantly impacts the health and productivity of small ruminants. The burden of parasitism and the escalating incidence of anthelmintic resistance necessitate alternative control methods. Here, we characterize the enzymatic activities of five mammalian cell-expressed recombinant H. contortus cysteine proteases (HcCPs), which include two cathepsin B-like proteins (HcCBP1 and HcCBP2) and three cysteine protease 1 proteins (HcCP1a, HcCP1b, and HcCP1c). We hypothesize that these enzymes degrade host blood proteins, thereby facilitating the parasite's nutrient acquisition and survival. Using synthetic cathepsin (cat) substrates, we show that HcCBP2 was the only protein that exhibited high catB/L but low cat

SUBMITTER: Karunakaran AC 

PROVIDER: S-EPMC12732675 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature