Ultrastructural evidence for the destruction of Schistosoma mansoni sporocysts associated with elevated lysosomal enzyme levels in Biomphalaria glabrata.
The activity levels of serum acid phosphtase, aminopeptidase, and lysozyme in a Brazilian strain of Biomphalaria glabrata were ascertained at 1, 2, and 3 hr after mechanical wounding or injection with albumin on the 30th day postexposure to a compatible strain of Schistosoma mansoni miracidia and found to be elevated. Parallel transmission electron microscope studies on daughter sporocysts and developing cercariae at these time intervals revealed progressive disintegration of the parasites that was associated with increased numbers of host granulocytes abutting the sporocyst surfaces. Furthermore, host granulocytes were observed to have passed through eroded sporocyst walls and attacked developing cercarial embryos. It is proposed that the elevated levels of lysosomal hydrolases released from activated host granulocytes as a result of challenge altered the parasite's surfaces so that these were recognized as nonself. Consequently, additional host granulocytic response, which included additional release of lysosomal enzymes into serum as well as phagocytosis of remnants of both sporocysts and developing cercariae, was elicited.
Cheng
T C
TC
Marine Biomedical Research Program, Medical University of South Carolina, Charleston 29412.
Dougherty
W J
WJ
D000135:Acid Phosphatase / Q000378:metabolism; D000626:Aminopeptidases / Q000378:metabolism; D000818:Animals; D001700:Biomphalaria / Q000469:parasitology*; D008247:Lysosomes / Q000201:enzymology*; D008854:Microscopy, Electron; D009113:Muramidase / Q000378:metabolism; D012550:Schistosoma mansoni / Q000378:metabolism* / Q000648:ultrastructure
D000135:Acid Phosphatase; D009113:Muramidase; D000626:Aminopeptidases