title: Plasmodium falciparum merozoite surface protein 1.
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.
authors.affiliation: Department of Pathology, Centre médical universitaire, Geneva, Switzerland. Daniel.Hoessli@medecine.unige.ch
authors.forename: Daniel C
authors.initials: DC
authors.lastname: Hoessli
authors.forename: Monique
authors.initials: M
authors.lastname: Poincelet
authors.forename: Ramneek
authors.initials: R
authors.lastname: Gupta
authors.forename: Subburaj
authors.initials: S
authors.lastname: Ilangumaran
authors.lastname: Nasir-ud-Din
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D004912:Erythrocytes / Q000378:metabolism; D006031:Glycosylation; D016778:Malaria, Falciparum / Q000378:metabolism; D020066:Merozoite Surface Protein 1 / Q000737:chemistry*; D017830:Octoxynol / Q000378:metabolism; D010963:Plasmodium falciparum / Q000737:chemistry*; D011499:Protein Processing, Post-Translational / Q000502:physiology; D022161:Transport Vesicles / Q000378:metabolism
chemical_list: D020066:Merozoite Surface Protein 1; D017830:Octoxynol