Suppression of macrophage lysosomal enzymes after Leishmania donovani infection

Abstract

In order to have an insight into the role of host lysosomal enzymes in the intracellular survival of Leishmania parasites, the activities of β-galactosidase, α-mannosidase, and N-acetyl-β-d-glucosaminidase were studied in peritoneal macrophages of hamsters infected with L. donovani. There was a significant decrease of all three lysosomal enzymes after infection. Heat-killed or formalintreated parasites failed to inhibit the enzymes, instead a slight stimulation was observed. Purified excreted factor from promastigotes had no effect on the enzymes except β-galactosidase which was inhibited up to 20%. Inhibition of enzymes was not due to increased secretion after infection. The absence of induction of any endogenous macrophage inhibitor was confirmed by mixed experiments. The levels of 5'-nucleotidase and lactate dehydrogenase remained unchanged after infection. Thus, the inhibition of lysosomal enzymes appears to be the effect of infection process and reflects to actual decrease rather than increased secretion or the action of any inhibitors present in Leishmania promastigotes.