Structural analysis of the glycosyl-phosphatidylinositol membrane anchor of the merozoite surface proteins-1 and -2 of Plasmodium falciparum
- Author(s)
- Gerold, P; Schofield, L; Blackman, MJ; Holder, AA; Schwarz, RT;
- Details
- Publication Year 1996-01,Volume 75,Issue #2,Page 131-143
- Journal Title
- MOLECULAR AND BIOCHEMICAL PARASITOLOGY
- Publication Type
- Journal Article
- Abstract
- Plasmodium falciparum accumulates the two merozoite surface proteins-1 and -2 during schizogony. Both proteins are proposed to be anchored in membranes by glycosyl-phosphatidylinositol membrane anchors. In this report the identity of these GPI-anchors is confirmed by labelling with tritiated precursors and additionally by specific enzymatic and chemical treatments. Detailed structural analysis of the core-glycans showed that the GPI-anchors of both proteins possess an extra alpha 1-2 linked mannose at the conserved trimannosyl-core-glycan. MSP-1 and MSP-2 labelled with tritiated myristic acid possess primarily radioactive myristic acid at inositol rings in both GPI-anchors. Additionally the hydrophobic fragments released from [H-3]myristic acid labelled GPI-anchors were identified as diacyl-glycerols, carrying preferentially [3H]palmitic acid in an ester-linkage.
- Publisher
- ELSEVIER SCIENCE BV
- Keywords
- TUMOR-NECROSIS-FACTOR; TOXOPLASMA-GONDII; GLYCOLIPID PRECURSORS; RESISTANT GLYCOLIPIDS; SIGNAL TRANSDUCTION; MALARIA; IDENTIFICATION; PHOSPHOLIPASE; GLYCOPROTEIN; BIOSYNTHESIS
- Publisher's Version
- https://doi.org/10.1016/0166-6851(95)02518-9
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 1996-01-01 12:00:00