Identification of two integral membrane proteins of Plasmodium falciparum.
AUTOR(ES)
Smythe, J A
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=281715Documentos Relacionados
- Integral membrane protein located in the apical complex of Plasmodium falciparum.
- Homologous genes encode two distinct histidine-rich proteins in a cloned isolate of Plasmodium falciparum.
- Unidirectional dominance of cytoplasmic inheritance in two genetic crosses of Plasmodium falciparum.
- Antigenic variation in Plasmodium falciparum.
- Protective immunity induced in Aotus monkeys by recombinant SERA proteins of Plasmodium falciparum.