Identification of the parasite transferrin receptor of Plasmodium falciparum-infected erythrocytes and its acylation via 1,2-diacyl-sn-glycerol. | Zendy

Kasturi Haldar | Zendy; C L Henderson | Zendy; George Cross | Zendy

Open Access

Identification of the parasite transferrin receptor of Plasmodium falciparum-infected erythrocytes and its acylation via 1,2-diacyl-sn-glycerol.

Author(s) -

Kasturi Haldar,

C L Henderson,

George Cross

Publication year - 1986

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.83.22.8565

Subject(s) - polyclonal antibodies , antiserum , plasmodium falciparum , transferrin , biology , transferrin receptor , receptor , epitope , biochemistry , microbiology and biotechnology , antibody , monoclonal antibody , malaria , immunology

The transferrin receptor of schizont-infected erythrocytes of Plasmodium falciparum (Gambian clone FCR-3/A2) is a parasite-encoded protein of Mr 102,000, which is present in purified erythrocyte membranes. Polyclonal antiserum to the purified Mr 102,000 protein was raised in rabbits. At physiological pH, immunoaffinity-purified protein bound human ferrotransferrin but not apotransferrin. Conversely, antibody to human transferrin was used to purify the ferrotransferrin-receptor complex from infected cells. The isolated receptor was specifically recognized by the polyclonal rabbit antiserum raised against the Mr 102,000 protein. Preliminary analysis indicated that, unlike the human receptor, the plasmodial transferrin receptor is not a disulfide linked dimer but a single polypeptide acylated via 1,2-diacyl-sn-glycerol.

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