Altered response of oyster hemocytes to Haplosporidium nelsoni (MSX) plasmodia treated with enzymes or metabolic inhibitors.
To avoid phagocytosis, parasites may mask themselves with host-like molecules that prevent recognition as nonself or they may produce substances that interfere with host cellular defenses. The protozoan parasite Haplosporidium nelsoni, which causes MSX disease in the eastern oyster Crassostrea virginica, is not ingested by host hemocytes. To assess potential avoidance mechanisms, oyster hemocytes were incubated with plasmodial stages of the parasite that had been pretreated with one of a variety of enzymes (proteases and carbohydrases) to alter surface molecules or with metabolic inhibitors to prevent the synthesis or active uptake of "masking" molecules, as well as the production and discharge of inhibitory substances. The maximum increase in phagocytosis resulting from treatment with carbohydrases was 12.5% (beta-galactosidase) and with proteases was 18% (Proteinase K). Inhibitors of aerobic metabolism resulted in a similar level of enhancement. In contrast, treatment of parasites with the glycolysis inhibitor iodoacetate enhanced phagocytosis by up to 66%. Thus, the process that obstructs phagocytosis involves aerobic and, especially, anaerobic pathways. The greater effect of a metabolic inhibitor compared to enzymes suggests that the mechanism involves more than just surface modification and may include the production of interference molecules.
Department of Marine and Coastal Sciences and New Jersey Agricultural Experiment Station, Haskin Shellfish Research Laboratory, Rutgers University, 6959 Miller Avenue, Port Norris, New Jersey, 08349, USA.
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Ford
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Ashton-Alcox
D000818:Animals; D004791:Enzyme Inhibitors; D056890:Eukaryota / Q000276:immunology*; D006434:Hemocytes / Q000276:immunology* / Q000469:parasitology; D006867:Hydrolases; D007461:Iodoacetates; D010125:Ostreidae / Q000276:immunology*; D010587:Phagocytosis / Q000276:immunology*
D004791:Enzyme Inhibitors; D007461:Iodoacetates; D006867:Hydrolases