A 170kDa multi-domain cystatin of Fasciola gigantica is active in the male reproductive system

Geadkaew, Amornrat; Kosa, Nanthawat; Siricoon, Sinee; Grams, Suksiri Vichasri; Grams, Rudi

doi:10.1016/j.molbiopara.2014.08.004

Cited by 16 publications

(21 citation statements)

References 25 publications

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“…Within the (adult) parasite tissues, FhStf-1 was detected in the surface lamella of the gut and in the reproductive organs, localizations that coincide with those previously reported for the cathepsin L s (Dalton et al 2003; Collins et al 2004; Zawistowska-Deniziak et al 2013), suggesting that part of the biological role of this inhibitor may be to control cathepsin L activity. The F. gigantica orthologue of the mentioned F. hepatica multidomain cystatin was predominantly localized in testis and sperm (Geadkaew et al 2014), supporting the relevance of Fasciola cystatins in reproduction.…”

Section: Discussionmentioning

confidence: 86%

Functional characterization of single-domain cystatin-like cysteine proteinase inhibitors expressed by the trematodeFasciola hepatica

et al. 2017

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Cystatins are small, phylogenetically conserved proteins that are tight-binding inhibitors of cysteine proteinases. The liver fluke Fasciola hepatica uses a diverse set of cysteine proteinases of the papain superfamily for host invasion, immune evasion and nutrition, but little is known about the regulation of these enzymes. The aim of this work is to characterize the cystatin repertoire of F. hepatica. For this purpose, we first surveyed the available sequence databases, identifying three different F. hepatica single-domain cystatins. In agreement with the in silico predictions, at least three small proteins with cysteine proteinase binding activity were identified. Phylogenetic analyses showed that the three cystatins (named FhStf-1, -2 and -3) are members of the I25A subfamily (stefins). Whereas FhStf-1 grouped with classical stefins, FhStf-2 and 3 fell in a divergent stefin subgroup unusually featuring signal peptides. Recombinant rFhStf-1, -2 and -3 had potent inhibitory activity against F. hepatica cathepsin L cysteine proteinases but differed in their capacity to inhibit mammalian cathepsin B, L and C. FhStf-1 was localized in the F. hepatica reproductive organs (testes and ovary), and at the surface lamella of the adult gut, where it may regulate cysteine proteinases related with reproduction and digestion, respectively. FhStf-1 was also detected among F. hepatica excretion-secretion (E/S) products of adult flukes. This suggests that it is secreted by non-classical secretory pathway and that it may interact with host lysosomal cysteine proteinases.

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Section: Discussionmentioning

confidence: 86%

Functional characterization of single-domain cystatin-like cysteine proteinase inhibitors expressed by the trematodeFasciola hepatica

et al. 2017

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“…For more information, visit (). Although these classifications are in most cases very useful, for some cystatins can be difficult to apply because there are combinations of different features that may not be attributed to one or other family (Ilgova et al ., 2017), or multidomain cystatins that albeit of high molecular weight (170 kDa), tandem cystatin repeats and degenerated core motifs still resemble type 2 cystatins (Geadkaew et al ., 2014).…”

Section: Molecular and Genetic Aspects Of A Lumbricoides Cystatinsmentioning

confidence: 99%

Helminth-derived cystatins: the immunomodulatory properties of an Ascaris lumbricoides cystatin

2021

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“…Recombinant FgCatL-A (UniProt: Q9XYL8), FgCB5 (UniProt: A0A0U4HGR1), FgStefin-1 (UniProt: C6GC97), FgStefin-2 (UniProt: K4P3W9), FgMDC-d10 (UniProt: A0A097GX18), FgCaBP-1 (UniProt: Q45TR6), and FgDM9-2 (UniProt: A0A142BYJ5) were expressed as previously described. 19,[28][29][30][31][32] An equal amount of each recombinant protein (500 ng) and 3 μg of F. gigantica CWE (positive control) were dotted onto a nitrocellulose membrane and air-dried. Pooled human fascioliasis antisera (1:100) were used to probe the membrane-bound antigens at 4°C overnight.…”

Section: Methodsmentioning

confidence: 99%

Evaluation of a Commercial Enzyme-Linked Immunosorbent Assay Kit and In-House Fasciola gigantica Cysteine Proteinases-Based Enzyme-Linked Immunosorbent Assays for Diagnosis of Human Fascioliasis

Tran

Intuyod

et al. 2019

The American Journal of Tropical Medicine and Hygiene

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Fascioliasis, caused by Fasciola hepatica and Fasciola gigantica infection, is a major food-borne trematodiasis in many places of the world, with the central region of Vietnam being reported as a highly endemic area. Stool examination for Fasciola eggs is not a sensitive method, and immunodiagnostic methods are preferable. We investigated various enzyme-linked immunosorbent assays (ELISAs) to evaluate their efficacy for fascioliasis diagnosis. Test sera used are primarily screened using an ELISA kit produced in Vietnam (VN kit; Viet Sinh Chemical Producing & Trading Co. Ltd., Ho Chi Minh City, Vietnam): Seropositive individuals having symptoms compatible with fascioliasis were regarded as clinically diagnosed fascioliasis cases. A commercial Fasciola IgG ELISA kit from Diagnostic Automation/Cortez Diagnostics, Inc. (USA kit; Woodland Hills, CA), which has been commonly used in Vietnam, was assessed and compared with in-house ELISA systems, including a cystatincapture (CC) ELISA using crude worm extract (CWE) and an indirect ELISA using a synthetic peptide Ac-TPTCHWECQVGYNKTYDEE-NHMe designed from the F. gigantica cathepsin B (FgCB5) molecule. The USA kit was suitable for routine diagnosis after recalibration of the manufacturer's suggested cutoff point. Cystatin-capture ELISA with CWE provided good sensitivity and specificity with perfect agreement to the results of the USA kit. In dotblot ELISA, recombinant FgCB5 reacted more strongly with human antisera than did other F. gigantica antigens tested. Enzyme-linked immunosorbent assay using the synthetic peptide fragment of the FgCB5 exhibited nearly 80% sensitivity and specificity, but the test results showed low agreement with CC-ELISA or the USA kit. In conclusion, the commercially available Fasciola IgG ELISA kit from the United States and the in-house CC ELISA using CWE are suitable for practical diagnosis for fascioliasis.

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A 170kDa multi-domain cystatin of Fasciola gigantica is active in the male reproductive system

Cited by 16 publications

References 25 publications

Functional characterization of single-domain cystatin-like cysteine proteinase inhibitors expressed by the trematodeFasciola hepatica

Functional characterization of single-domain cystatin-like cysteine proteinase inhibitors expressed by the trematodeFasciola hepatica

Helminth-derived cystatins: the immunomodulatory properties of an Ascaris lumbricoides cystatin

Evaluation of a Commercial Enzyme-Linked Immunosorbent Assay Kit and In-House Fasciola gigantica Cysteine Proteinases-Based Enzyme-Linked Immunosorbent Assays for Diagnosis of Human Fascioliasis

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