IDENTIFICATION OF 2 INTEGRAL MEMBRANE-PROTEINS OF PLASMODIUM-FALCIPARUM

被引：246

作者：

SMYTHE, JA ^{[1
]}

COPPEL, RL ^{[1
]}

BROWN, GV ^{[1
]}

RAMASAMY, R ^{[1
]}

KEMP, DJ ^{[1
]}

ANDERS, RF ^{[1
]}

机构：

[1] QUEENSLAND INST MED RES, BRISBANE 4006, AUSTRALIA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1988年 / 85卷 / 14期

关键词：

D O I：

10.1073/pnas.85.14.5195

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

We describe the isolation and cloning of two integral membrane protein antigens of Plasmodium falciparum. The antigens were isolated by Triton X-114 temperature-dependent phase separation, electrophoretically transferred to nitrocellulose, and used to affinity-purify monospecific human antibodies. These antibodies were used to isolate the corresponding cDNA clones from a phage .lambda.gt11-Amp3 cDNA expression library. Clone Ag512 corresponds to a Mr 55,000 merozoite rhoptry antigen, and clone Ag513 corresponds to a Mr 45,000 merozoite surface antigen. Both proteins can be biosynthetically labeled with [3H]glucosamine and [3H]myristic acid, suggesting that they may be anchored in membranes via a glycosylphosphatidylinositol moiety. Similarities in the C-terminal sequences of the Mr 45,000 merozoite surface antigen and the Trypanosoma brucei variant surface glycoproteins provides further evidence that this antigen has a glycosylphosphatidylinositol anchor.

引用

页码：5195 / 5199

页数：5

共 34 条

[31] CODON USAGE IN PLASMODIUM-FALCIPARUM [J].