Acylation of a Plasmodium falciparum merozoite surface antigen via sn-1,2-diacyl glycerol

Kasturi Haldar, Michael A. J. Ferguson, George A. M. Cross

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    105 Citations (Scopus)

    Abstract

    The 195-kDA merozoite protein synthesized in schizonts of Plasmodium falciparum (Holder, A. A., and Freeman, R. R. (1982) J. Exp. Med. 156, 1528-1538) contains ester-linked fatty aid. Enzymatic treatment of the purified acylated protein established that the lipid is present as sn-1,2-diacyl glycerol, most probably linked to a phosphodiester at the 3-position of glycerol. The phosphodiglyceride is not directly esterified to an amino acid residue on the polypeptide backbone. The 195-kDa protein is processed to three fragments (83, 42, and 19 kDa) on the surface of free merozoites (Holder, A. A., and Freeman, R. R. (1984) J. Exp. Med. 160, 624-629), of which only the 42-kDa polypeptide is acylated.

    Original languageEnglish
    Pages (from-to)4969-4974
    Number of pages6
    JournalJournal of Biological Chemistry
    Volume260
    Issue number8
    Publication statusPublished - 25 Apr 1985

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