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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Analysis of recombinant merozoite surface protein-1 of Plasmodium falciparum expressed in mammalian cells.

Synthetic chimeric DNA constructs with a reduced A + T content coding for full-length merozoite surface protein-1 of Plasmodium falciparum (MSP1) and three fragments thereof were expressed in HeLa cells. To target the recombinant proteins to the surface of the host cell the DNA sequences coding for the N-terminal signal sequence and for the putative C-terminal recognition/attachment signal for the glycosyl-phosphatidyl-inositol (GPI)-anchor of MSP1 were replaced by the respective DNA sequences of the human decay-accelerating-factor ( DAF). The full-length recombinant protein, hu-MSP1- DAF, was stably expressed and recognised by monoclonal antibodies that bind to the N-terminus or the C-terminus of the native protein, respectively. Its apparent molecular mass is higher as compared to the native protein and it is post-translationally modified by attachment of N-glycans whereas native MSP1 is not glycosylated. Immunofluorescence images of intact cells show a clear surface staining. After permeabilization hu-MSP1- DAF can be detected in the cytosol as well. As judged by protease treatment of intact cells 25% of recombinant MSP1 is located on the surface. This fraction of hu-MSP1- DAF can be cleaved off the cell membrane by phosphatidylinositol-specific phospholipase C indicating that the protein is indeed bound to the cell membrane via a GPI-anchor. Human erythrocytes do not adhere to the surface of mammalian cells expressing either of the constructs made in this study.[1]


  1. Analysis of recombinant merozoite surface protein-1 of Plasmodium falciparum expressed in mammalian cells. Burghaus, P.A., Gerold, P., Pan, W., Schwarz, R.T., Lingelbach, K., Bujard, H. Mol. Biochem. Parasitol. (1999) [Pubmed]
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