Structural analysis of the glycosyl-phosphatidylinositol membrane anchor of the merozoite surface proteins-1 and -2 of Plasmodium falciparum

被引：164

作者：

Gerold, P

Schofield, L

Blackman, MJ

Holder, AA

Schwarz, RT

机构：

[1] UNIV MARBURG, ZENTRUM HYG & MED MIKROBIOL, D-35037 MARBURG, GERMANY

[2] ROYAL MELBOURNE HOSP, WALTER & ELIZA HALL INST MED RES, PARKVILLE, VIC 3050, AUSTRALIA

[3] NATL INST MED RES, LONDON NW7 1AA, ENGLAND

来源：

MOLECULAR AND BIOCHEMICAL PARASITOLOGY | 1996年 / 75卷 / 02期

基金：

英国医学研究理事会;

关键词：

Plasmodium falciparum; MSP-1; MSP-2; glycosyl-phosphatidylinositol;

D O I：

10.1016/0166-6851(95)02518-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：131 / 143

页数：13

共 40 条

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