ArticleThe Journal of biological chemistry2008
Structural and functional relationships in the virulence-associated cathepsin L proteases of the parasitic liver fluke, Fasciola hepatica.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 101 citations in OpenAlex.
- Proteomic characterization of adult Fasciola gigantica recovered from naturally infected buffaloes in Punjab Pakistan.PloS one · 2026Article
- In silico design of an epitope-based vaccine ensemble for fasliolopsiasis.Frontiers in genetics · 2024Article
- Molecular characterization of EcCLP1, a new putative cathepsin L protease from Echinococcus canadensis.Parasite (Paris, France) · 2024Article
- Exploring Evolutionary Relationships within Neodermata Using Putative Orthologous Groups of Proteins, with Emphasis on Peptidases.Tropical medicine and infectious disease · 2023Article
- Article
- Molecular characterization and determination of the biochemical properties of cathepsin L of Trichinella spiralis.Veterinary research · 2022Article
- Article
- Structure determinants defining the specificity of papain-like cysteine proteases.Computational and structural biotechnology journal · 2022Review
- The Zoonotic Helminth ParasiteAnimals : an open access journal from MDPI · 2021Article
- Trematode Proteomics: Recent Advances and Future Directions.Pathogens (Basel, Switzerland) · 2021Review
- Differences in the antibody response to adult Fasciola hepatica excretory/secretory products in experimentally and naturally infected cattle and sheep.Veterinary parasitology · 2021Article
- Regulation of the Fasciola hepatica newly excysted juvenile cathepsin L3 (FhCL3) by its propeptide: a proposed 'clamp-like' mechanism of binding and inhibition.BMC molecular and cell biology · 2020Article
- An atypical and functionally diverse family of Kunitz-type cysteine/serine proteinase inhibitors secreted by the helminth parasite Fasciola hepatica.Scientific reports · 2020Article
- Identification of protective peptides of Fasciola hepatica-derived cathepsin L1 (FhCL1) in vaccinated sheep by a linear B-cell epitope mapping approach.Parasites & vectors · 2020Article
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- Cathepsin L3 FromFrontiers in immunology · 2019Article
- Cysteine peptidases of Eudiplozoon nipponicum: a broad repertoire of structurally assorted cathepsins L in contrast to the scarcity of cathepsins B in an invasive species of haematophagous monogenean of common carp.Parasites & vectors · 2018Article
- Substrate Specificity of Cysteine Proteases Beyond the SFrontiers in molecular biosciences · 2018Article
- Unexpected Activity of a Novel Kunitz-type Inhibitor: INHIBITION OF CYSTEINE PROTEASES BUT NOT SERINE PROTEASES.The Journal of biological chemistry · 2016Article
- Structural and Functional Characterization of the Major Allergen Amb a 11 from Short Ragweed Pollen.The Journal of biological chemistry · 2016Article
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Authors and funding
15 authors at 3 institutions in 3 countries.
Funding
Abstract
The helminth parasite Fasciola hepatica secretes cysteine proteases to facilitate tissue invasion, migration, and development within the mammalian host. The major proteases cathepsin L1 (FheCL1) and cathepsin L2 (FheCL2) were recombinantly produced and biochemically characterized. By using site-directed mutagenesis, we show that residues at position 67 and 205, which lie within the S2 pocket of the active site, are critical in determining the substrate and inhibitor specificity. FheCL1 exhibits a broader specificity and a higher substrate turnover rate compared with FheCL2. However, FheCL2 can efficiently cleave substrates with a Pro in the P2 position and degrade collagen within the triple helices at physiological pH, an activity that among cysteine proteases has only been reported for human cathepsin K. The 1.4-A three-dimensional structure of the FheCL1 was determined by x-ray crystallography, and the three-dimensional structure of FheCL2 was constructed via homology-based modeling. Analysis and comparison of these structures and our biochemical data with those of human cathepsins L and K provided an interpretation of the substrate-recognition mechanisms of these major parasite proteases. Furthermore, our studies suggest that a configuration involving residue 67 and the "gatekeeper" residues 157 and 158 situated at the entrance of the active site pocket create a topology that endows FheCL2 with its unusual collagenolytic activity. The emergence of a specialized collagenolytic function in Fasciola likely contributes to the success of this tissue-invasive parasite.
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