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Enzymatic effect of hypodermin A, a parasite protease, on bovine lymphocyte membrane antigens
Author(s) -
Moiré Nathalie,
NicolasGaulard Isabelle,
Le Vern Yves,
Boulard Chantal
Publication year - 1997
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 - 10.1046/j.1365-3024.1997.d01-139.x
Subject(s) - biology , antigen , phytohaemagglutinin , lymphocyte , protease , antibody , immune system , microbiology and biotechnology , pmsf , immunology , enzyme , biochemistry
The protease hypodermin A (HA) is produced by the parasitic warble‐fly larva and is implicated in the modulation of the bovine immune system. This study examines the effect of this enzyme on the cell surface markers of bovine lymphocytes. HA interfered with the binding of all anti‐lymphocyte receptor antibodies tested. Anti‐BoCD2 and CD5 staining was completely abolished. But the mean fluorescence intensity (MFI) only was diminished for antibodies against BoCD4, CD8 and CD18. On the contrary, the MFI for anti‐MHC Cl I molecules staining was increased. This effect of HA began as early as one h, and was reversed by removal of HA. Heating or PMSF treatment, which both inhibit protease activity, abolished the action of HA on the surface antigens. The HA concentrations (100 μg/ml) needed to alter antibody binding were similar to those that inhibited phytohaemagglutinin (PHA)‐induced proliferation. These results show that enzymatic activity of HA on lymphocyte surface markers may be implicated in the inhibition of lymphocyte proliferation.