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Neutralization of the activity of a Fasciola hepatica cathepsin L proteinase by anti‐cathepsin L antibodies
Author(s) -
SMITH ANGELA M.,
CARMONA CARLOS,
DOWD ANDREW J.,
McGONIGLE SHARON,
ACOSTA DANIEL,
DALTON JOHN P.
Publication year - 1994
Publication title -
parasite immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.795
H-Index - 75
eISSN - 1365-3024
pISSN - 0141-9838
DOI - 10.1111/j.1365-3024.1994.tb00356.x
Subject(s) - fasciola hepatica , cathepsin , cathepsin l1 , cathepsin l , cathepsin b , biology , antibody , cathepsin d , microbiology and biotechnology , enzyme , immunology , biochemistry , helminths
SUMMARY Fasciola hepatica secretes a cathepsin L proteinase that is suggested to play an in vivo role in immunoprotection since the enzyme can cleave host immunoglobulin. In the present report, rabbit anti‐cathepsin L IgG was shown to bind to the cathepsin L enzyme and inhibit its ability to cleave IgG molecules. Cathepsin L can prevent the antibody‐mediated attachment of eosinophils to newly excysted juveniles in in vitro assays; however, if anti‐cathepsin L IgG are mixed with the cathepsin L prior to the addition of the enzyme to the assay, eosinophils attach to the newly excysted juveniles. Thus it is possible to prepare antibodies that can bind and disrupt the biological activity of the F. hepatica cathepsin L.