Abstract
Cathepsin peptidases form a major component of the secreted proteins of the blood-feeding trematodes Fasciola hepatica and Schistosoma mansoni. These peptidases fulfill many functions, from facilitating infection to feeding and immune evasion. In this study, we examined the Fasciola cathepsin L peptidases FhCL1, FhCL2, and FhCL3 and the schistosomal cathepsin peptidases SmCB1 and SmCL3 for their anticoagulant properties. Although no direct anticoagulant effect of these peptidases was observed, we discovered that cathepsin peptidases from Fasciola, but not from Schistosoma, were able to degrade purified fibrinogen, with FhCL1 having the highest fibrinogenolytic activity. Additionally, FhCL1 and FhCL2 both efficiently degraded fibrin. The lack of a direct anticoagulant or fibrinolytic effect of these peptidases is explained by their inhibition by plasma components. However, within the parasite gut, high concentrations of these peptidases could induce an anticoagulant environment, facilitating blood-feeding for extended periods.
Original language | English |
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Pages (from-to) | 10-13 |
Number of pages | 4 |
Journal | Molecular and Biochemical Parasitology |
Volume | 221 |
DOIs | |
Publication status | Published - 1 Apr 2018 |
Funding
The Fasciola hepatica and Schistosome mansoni purified recombinant peptidases were a gift from Prof. John P. Dalton's laboratory, Queen's University Belfast, Northern Ireland. This work was supported by the Netherlands organization for scientific research (NWO) and the Erasmus postgraduate school Molecular Medicine (MolMed) [Erasmus Graduate Programme Infection & Immunity, NWO file number: 022.005.032].
Keywords
- Cathepsin peptidases
- Fasciola hepatica
- Fibrin
- Fibrinogen
- Schistosoma mansoni