Abstract
Human red blood cells (RBC) were infected with the malarial parasite Plasmodium falciparum, the anchoring of schizont proteins to RBC membranes by glycoinositol phospholipids was demonstrated by three criteria: (1) metabolic incorporation of 3H-ethanolamine and 3H-myristate into the protein; (2) release of 35S-methionine-labelled protein into the supernatant after incubation with phosphatidylinositol-specific phospholipase C; and (3) the exposure of a glycoinositol phosphate epitope on the methionine-labelled protein following phospholipase C cleavage. Labelled proteins were analysed by immunoprecipitation, polyacrylamide gel electrophoresis in sodium dodecylsulphate and gel fluorography. Several candidate proteins were observed when each criteria was investigated. Among these, 3 proteins which met all three criteria were identified by immunoprecipitation with monospecific sera or monoclonal antibodies. These included 3 possible vaccine candidates, the p190 major surface antigen, the p76 serine protease and the p71 protein which is thought to be a member of the family of heat-shock Hsp70 proteins.
Original language | English (US) |
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Pages (from-to) | 743-755 |
Number of pages | 13 |
Journal | Research in Immunology |
Volume | 141 |
Issue number | 7 |
DOIs | |
State | Published - 1990 |
Keywords
- Glycolipid
- Malaria
- Phospholipids
- Plasmodium falciparum
- Proteins
- RBC anchoring
- Surface antigen
- Vaccination
ASJC Scopus subject areas
- Immunology