Extracellular killing of Trypanosoma cruzi amastigotes by human eosinophils.
Granules released from human eosinophils upon interaction with Trypanosoma cruzi amastigotes in vitro were seen attached to the surface of non-internalized parasites by electron microscopy. Amastigote damage was preceded by the binding of eosinophil granule material to its membrane, and eosinophil granule major basic protein (MBP) bound to the parasite surface was readily detectable. Additional evidence of eosinophil cytotoxicity for extracellular amastigotes was the observation that amastigotes trapped between two eosinophils, without being ingested by either one, were destroyed at the interface. Amastigotes isolated from the spleens of infected mice or grown in culture were similarly sensitive to the lytic effects of purified MBP. These results demonstrate the ability of human eosinophils to lyse T. cruzi amastigotes extracellularly in the absence of antibody and suggest that MBP may be involved in the effect. Thus, eosinophils, known to be capable of destroying phagocytosed amastigotes, could also contribute to the clearance of these parasites through extracellular killing.
Villalta
F
F
Department of Microbiology and Public Health, Michigan State University, East Lansing 48824-1101.
Pankratz
H S
HS
Kierszenbaum
F
F
D000818:Animals; D001798:Blood Proteins / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism / Q000648:ultrastructure; D047091:Eosinophil Granule Proteins; D004804:Eosinophils / Q000276:immunology* / Q000469:parasitology / Q000648:ultrastructure; D006801:Humans; D008854:Microscopy, Electron; D010587:Phagocytosis; D011485:Protein Binding; D012260:Ribonucleases; D014349:Trypanosoma cruzi / Q000276:immunology* / Q000378:metabolism / Q000648:ultrastructure
D001798:Blood Proteins; D047091:Eosinophil Granule Proteins; D012260:Ribonucleases