Neutralization of the activity of a Fasciola hepatica cathepsin L proteinase by anti-cathepsin L antibodies.

Abstract:

: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.

journal_name

Parasite Immunol

journal_title

Parasite immunology

authors

Smith AM,Carmona C,Dowd AJ,McGonigle S,Acosta D,Dalton JP

doi

10.1111/j.1365-3024.1994.tb00356.x

subject

Has Abstract

pub_date

1994-06-01 00:00:00

pages

325-8

issue

6

eissn

0141-9838

issn

1365-3024

journal_volume

16

pub_type

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