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Proteinases secreted by Fasciola hepatica degrade extracellular matrix and basement membrane components
P Berasaín1, F Goñi, S McGonigle
1Unidad de Biologia Parasitaria, Instituto de Higiene, Montevideo, Uruguay.
Abstract:
The invasive stages of the parasitic trematode Fasciola hepatica release proteinases into the medium in which they are maintained. In this study, we investigated the interaction of F. hepatica excretory/secretory (E/S) products and 2 cysteine proteinases (CL1 and CL2) purified from these products with extracellular matrix and basement membrane macromolecules. Fasciola hepatica E/S products contained collagenolytic activity on fibrillar types I and III collagen as well as basement membrane type IV collagen. CL1 and CL2 were capable of degrading acid-soluble type III and type IV collagen but not insoluble type I collagen. In contrast, neither the E/S products nor the purified CL1 and CL2 showed elastinolytic activity. Fibronectin and laminin were degraded by E/S products and by CL1 and CL2. Sequence analysis of fibronectin degradation products showed that the fragments obtained corresponded to complete biologically active domains. These results indicate that the cysteine proteinases secreted by F. hepatica may be involved in the process of tissue invasion by the parasite.
Insights
The parasitic fluke Fasciola hepatica secretes cysteine proteinases that degrade extracellular matrix components like collagen, fibronectin, and laminin. These enzymes likely aid the parasite
Area of Science:
- Parasitology
- Molecular Biology
- Biochemistry
Background:
- The invasive stages of Fasciola hepatica, a parasitic trematode, release proteinases.
- Understanding these proteinases is crucial for comprehending parasite invasion mechanisms.
Purpose of the Study:
- To investigate the interaction of Fasciola hepatica excretory/secretory (E/S) products and purified cysteine proteinases (CL1 and CL2) with extracellular matrix and basement membrane macromolecules.
- To determine the specific collagen types and other matrix proteins degraded by these enzymes.
Main Methods:
- Analysis of proteinase activity in F. hepatica E/S products.
- Purification and characterization of cysteine proteinases CL1 and CL2.
- Degradation assays using fibrillar collagens (types I and III), type IV collagen, elastin, fibronectin, and laminin.
- Sequence analysis of fibronectin degradation products.
Main Results:
- F. hepatica E/S products exhibited collagenolytic activity against types I, III, and IV collagen.
- Purified CL1 and CL2 degraded acid-soluble type III and type IV collagen but not insoluble type I collagen.
- Neither E/S products nor purified proteinases showed elastinolytic activity.
- Fibronectin and laminin were degraded by E/S products and by CL1 and CL2, yielding complete biologically active domains.
Conclusions:
- Fasciola hepatica cysteine proteinases (CL1 and CL2) can degrade key extracellular matrix components.
- These proteinases likely play a significant role in the parasite's tissue invasion process.
- The degradation of fibronectin and laminin suggests a mechanism for facilitating parasite migration through host tissues.