In vitro parasite-monocyte interactions in human leishmaniasis: effect of enzyme treatments on attachment.
Essential to the pathogenesis of leishmaniasis is the ability of Leishmania spp. to attach to mononuclear phagocyte surfaces before entering this host cell which they parasitize. We have investigated the attachment phase of infection in vitro by quantitating the percent of human peripheral blood monocytes pretreated with cytochalasin (to prevent parasite entry) to which tissue-derived L. tropica amastigotes will attach during coincubation at 37 degrees C in serum-free medium. We determined that pretreatment of parasites with trypsin, chymotrypsin, Pronase, and neuraminidase reduced attachment. In contrast, parasites treated with beta-galactosidase had an enhanced ability to attach to host cells. Treatment of monocytes with chymotrypsin and Pronase, but not with trypsin or neuraminidase, reduced attachment of untreated amastigotes. We propose that in vitro amastigote attachment under serum-free conditions depends on the interaction of protein determinants on the surface of both parasite and host cell.
D000818:Animals; D002918:Chymotrypsin / Q000494:pharmacology; D010450:Endopeptidases / Q000494:pharmacology*; D005696:Galactosidases / Q000494:pharmacology*; D006790:Host-Parasite Interactions; D006801:Humans; D007891:Leishmania / Q000502:physiology*; D007896:Leishmaniasis / Q000469:parasitology; D009000:Monocytes / Q000469:parasitology*; D009439:Neuraminidase / Q000494:pharmacology*; D011402:Pronase / Q000494:pharmacology; D014357:Trypsin / Q000494:pharmacology; D001616:beta-Galactosidase / Q000494:pharmacology*
D005696:Galactosidases; D009439:Neuraminidase; D001616:beta-Galactosidase; D010450:Endopeptidases; D002918:Chymotrypsin; D014357:Trypsin; D011402:Pronase