Plasmodium falciparum merozoite surface protein 1 - Glycosylation and localization to low-density, detergent-resistant membranes in the parasitized erythrocyte

D.C. Hoessli, M. Poincelet, Ramneek Gupta, S. Ilangumaran, Nasir -ud-Din

    Research output: Contribution to journalJournal articleResearchpeer-review

    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.
    Original languageEnglish
    JournalEuropean journal of biochemistry
    Volume270
    Issue number2
    Pages (from-to)366-375
    ISSN0014-2956
    Publication statusPublished - 2003

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