Neutralization of the activity of a Fasciola hepatica cathepsin L proteinase by anti-cathepsin L antibodies.
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.
School of Biological Sciences, Dublin City University, Republic of Ireland.
A M
AM
Smith
C
C
Carmona
A J
AJ
Dowd
S
S
McGonigle
D
D
Acosta
J P
JP
Dalton
D000818:Animals; D056668:Cathepsin L; D002403:Cathepsins / Q000378:metabolism*; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases; D004792:Enzyme Precursors / Q000276:immunology; D005210:Fasciola hepatica / Q000201:enzymology*; D007074:Immunoglobulin G / Q000378:metabolism; D009500:Neutralization Tests; D011817:Rabbits
D004792:Enzyme Precursors; D007074:Immunoglobulin G; D002403:Cathepsins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D056668:Cathepsin L