Identification of two integral membrane proteins of Plasmodium falciparum.

J. A. Smythe, R. L. Coppel, G. V. Brown, R. Ramasamy, D. J. Kemp, R. F. Anders

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Abstract

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.

Original languageEnglish
Pages (from-to)5195-5199
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume85
Issue number14
DOIs
Publication statusPublished - 1 Jan 1988
Externally publishedYes

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