Concurrent Inhibition by Tunicamycin of Glycosylation and Parasitemia in Malarial Parasites (Plasmodium falciparum) Cultured in Human Erythrocytes
- 1 January 1981
- journal article
- research article
- Published by S. Karger AG in Pharmacology
- Vol. 23 (3) , 165-170
- https://doi.org/10.1159/000137545
Abstract
Tunicamycin (0.1–10 μg/ml) incubated 96 h with human erythrocytes infected with malarial parasites significantly decreased parasitemia compared to controls. The anti-malarial effect of tunicamycin was dose-related and paralleled its inhibition of the incorporation of radiolabeled glucosamine into parasite-derived membrane macromolecules. Tunicamycin had no significant effect on isoleucine incorporation into parasite-derived macromolecules. These results suggest that tunicamycin may act by inhibition of the glycosylation of parasite macromolecules. The results also indicate the role of glycosylated macromolecules in the survival of the erythrocytic stage of Plasmodium falciparum and the potential for selective inhibitors of the glycosylation of parasite macromolecules as agents for malarial chemotherapy.Keywords
This publication has 7 references indexed in Scilit:
- LABELING OF MEMBRANE-GLYCOPROTEINS OF CULTIVATED PLASMODIUM-FALCIPARUM1980
- The Dolichol Pathway of Protein Glycosylation in Rat LiverEuropean Journal of Biochemistry, 1979
- Immunization against malaria with antigen from Plasmodium falciparum cultivated in vitro.Proceedings of the National Academy of Sciences, 1978
- Glycopeptides derived from individual membrane glycoproteins from control and Rous sarcoma virus-transformed hamster fibroblasts.Journal of Biological Chemistry, 1978
- Plasmodium falciparum in Culture: Use of Outdated Erythrocytes and Description of the Candle Jar MethodJournal of Parasitology, 1977
- Tunicamycin inhibits glycosylation and multiplication of Sindbis and vesicular stomatitis virusesJournal of Virology, 1977
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976