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Plasmodium falciparum merozoite surface protein 1

Poincelet, Monique
Gupta, Ramneek
Nasir ud, Din
Published in European Journal of Biochemistry. 2003, vol. 270, no. 2, p. 366-375
Abstract In addition to the major carbohydrate moieties of the glycosylphosphatidylinositol (GPI) anchor, we report that Plasmodium falciparum merozoite surface protein 1 (MSP-1) bears O-GlcNAc modifications predominantly in beta-anomeric configuration, in both the C- and N-terminal portions of the protein. Subcellular fractionation of parasitized erythrocytes in the late trophozoite/schizont stage reveals that GPI-anchored C-terminal fragments of MSP-1 are recovered in Triton X-100 resistant, low-density membrane fractions. Our results suggest that O-GlcNAc-modified MSP-1 N-terminal fragments tend to localize within the parasitophorous vacuolar membrane while GPI-anchored MSP-1 C-terminal fragments associate with low-density, Triton X-100 resistant membrane domains (rafts), redistribute in the parasitized erythrocyte and are eventually shed as membrane vesicles that also contain the endogenous, GPI-linked CD59.
Keywords AnimalsCell Membrane/metabolismErythrocytes/metabolismGlycosylationMalaria, Falciparum/metabolismMerozoite Surface Protein 1/ chemistryOctoxynol/metabolismPlasmodium falciparum/ chemistryProtein Processing, Post-Translational/physiologyTransport Vesicles/metabolism
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PMID: 12605687
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