ArticleScientific reports2020
An atypical and functionally diverse family of Kunitz-type cysteine/serine proteinase inhibitors secreted by the helminth parasite Fasciola hepatica.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 49 citations in OpenAlex.
- Evolution of the reproductive interactome and the origins of postmating-prezygotic reproductive divergence.BMC biology · 2026Article
- Roles and regulation of the Kunitz domain protein MLT-11 during C. elegans cuticle synthesis and molting.Genetics · 2026Article
- Dynamic shifts in isomiR profiles during parasite maturation ofRNA biology · 2025Article
- MLT-11 is necessary forbioRxiv : the preprint server for biology · 2025Article
- Lysosomal Proteases and Their Inhibitors.International journal of molecular sciences · 2024Article
- Antibody detection against Kunitz-type protein inInternational journal of veterinary science and medicine · 2023Article
- Article
- Targeting Secreted Protease/Anti-Protease Balance as a Vaccine Strategy against the HelminthVaccines · 2022Article
- Article
- Antigen-specific response of CD4Veterinary research · 2021Article
- The cnidarian parasitePeerJ · 2021Article
- Autonomous Non Antioxidant Roles forFrontiers in cellular and infection microbiology · 2021Review
- Immune Evasion Strategies of Schistosomes.Frontiers in immunology · 2020Review
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Fasciola hepatica is a global parasite of humans and their livestock. Regulation of parasite-secreted cathepsin L-like cysteine proteases associated with virulence is important to fine-tune parasite-host interaction. We uncovered a family of seven Kunitz-type (FhKT) inhibitors dispersed into five phylogenetic groups. The most highly expressed FhKT genes (group FhKT1) are secreted by the newly excysted juveniles (NEJs), the stage responsible for host infection. The FhKT1 inhibitors do not inhibit serine proteases but are potent inhibitors of parasite cathepsins L and host lysosomal cathepsin L, S and K cysteine proteases (inhibition constants < 10 nM). Their unusual inhibitory properties are due to (a) Leu
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