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J Proteome Res ; 21(8): 1997-2010, 2022 08 05.
Article in English | MEDLINE | ID: mdl-35849550

ABSTRACT

Fasciola hepatica, the common liver fluke and causative agent of zoonotic fasciolosis, impacts on food security with global economic losses of over $3.2 BN per annum through deterioration of animal health, productivity losses, and livestock death and is also re-emerging as a foodborne human disease. Cathepsin proteases present a major vaccine and diagnostic target of the F. hepatica excretory/secretory (ES) proteome, but utilization in diagnostics of the highly antigenic zymogen stage of these proteins is surprisingly yet to be fully exploited. Following an immuno-proteomic investigation of recombinant and native procathepsins ((r)FhpCL1), including mass spectrometric analyses (DOI: 10.6019/PXD030293), and using counterpart polyclonal antibodies to a recombinant mutant procathepsin L (anti-rFhΔpCL1), we have confirmed recombinant and native cathepsin L zymogens contain conserved, highly antigenic epitopes that are conformationally dependent. Furthermore, using diagnostic platforms, including pilot serum and fecal antigen capture enzyme-linked immunosorbent assay (ELISA) tests, the diagnostic capacities of cathepsin L zymogens were assessed and validated, offering promising efficacy as markers of infection and for monitoring treatment efficacy.


Subject(s)
Fasciola hepatica , Fascioliasis , Animals , Cathepsin L/genetics , Cathepsin L/metabolism , Enzyme Precursors , Enzyme-Linked Immunosorbent Assay/methods , Epitopes , Fasciola hepatica/chemistry , Fasciola hepatica/genetics , Fascioliasis/diagnosis , Humans
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