Journal article

Identification and stoichiometry of glycosylphosphatidylinositol-anchored membrane proteins of the human malaria parasite Plasmodium falciparum

Paul R Gilson, Thomas Nebl, Damjan Vukcevic, Robert L Moritz, Tobias Sargeant, Terence P Speed, Louis Schofield, Brendan S Crabb

Molecular & Cellular Proteomics | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2006


Most proteins that coat the surface of the extracellular forms of the human malaria parasite Plasmodium falciparum are attached to the plasma membrane via glycosylphosphatidylinositol (GPI) anchors. These proteins are exposed to neutralizing antibodies, and several are advanced vaccine candidates. To identify the GPI-anchored proteome of P. falciparum we used a combination of proteomic and computational approaches. Focusing on the clinically relevant blood stage of the life cycle, proteomic analysis of proteins labeled with radioactive glucosamine identified GPI anchoring on 11 proteins (merozoite surface protein (MSP)-1, -2, -4, -5, -10, rhoptry-associated membrane antigen, apical sushi pro..

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