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Biochimica et biophysica acta

Glycosylation reactions in Plasmodium falciparum, Toxoplasma gondii, and Trypanosoma brucei brucei probed by the use of synthetic peptides.


PMID 8280751

Abstract

Synthetic peptides were used to probe O- and N-glycosylation reactions in cell-free systems of the parasitic protozoa Plasmodium falciparum, Toxoplasma gondii, and Trypanosoma brucei brucei. O-Glycosylation of the peptide Pro-Tyr-Thr-Val-Val was observed with lysates from all organisms. However, the spectrum of sugars transferred from their respective nucleotide or dolichol-phosphate derivatives to the peptide varied greatly according to the parasite. N-glycosylation of the peptides N-Bz-Asn-Gly-ThrNH2 and DNP-Arg-Asn-Ala-Thr-Ala-ValNH2 by exogenous radioactive dolichol-pyrophosphate linked oligosaccharide donors was observed only when lysates of T. gondii or T. b. brucei were used, but not in P. falciparum. To assay for endogenous N-glycosylation donors, the radiolabeled tripeptide [3H]Ac-Asn-Gly-ThrNHMe was used as acceptor. The peptide was N-glycosylated only by T. gondii and T. b. brucei preparations. Only in these latter two parasites dolichol-cycle mannosyltransferase activity was demonstrated by the elongation of exogenous radiolabeled dolichol-PP-chitobiose. The data substantiate the occurrence of protein O-glycosylation in parasitic protozoa and the exceptional absence of protein N-glycosylation in the asexual intraerythrocytic stage of the malaria parasite, P. falciparum.

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