Partial structure of glutamic acid and alanine-rich protein, a major surface glycoprotein of the insect stages of Trypanosoma congolense

Lynn M. Thomson, Douglas J. Lamont, Angela Mehlert, J. David Barry, Michael A. J. Ferguson

    Research output: Contribution to journalArticle

    17 Citations (Scopus)

    Abstract

    The tsetse fly transmitted salivarian trypanosome, Trypanosoma congolense of the subgenus Nanomonas, is the most significant of the trypanosomes with respect to the pathology of livestock in sub-Saharan Africa. Unlike the related trypanosome Trypanosoma brucei of the subgenus Trypanozoon, the major surface molecules of the insect stages of T. congolense are poorly characterized. Here, we describe the purification and structural characterization of the glutamic acid and alanine-rich protein, one of the major surface glycoproteins of T. congolense procyclic and epimastigote forms. The glycoprotein is a glycosylphosphatidylinositol-anchored molecule with a galactosylated glycosylphosphatidylinositol anchor containing an sn-1-stearoyl-2-L-3-HPO4-1-(2-O-acyl)-D-myoinositol phospholipid moiety. The 21.6-kDa polypeptide component carries two large mannose- and galactose-containing oligosaccharides linked to threonine residues via phosphodiester linkages. Mass spectrometric analyses of tryptic digests suggest that several or all of the closely related glutamic acid and alanine-rich protein genes are expressed simultaneously in a T. congolense population growing in vitro.

    Original languageEnglish
    Pages (from-to)48899-48904
    Number of pages6
    JournalJournal of Biological Chemistry
    Volume277
    Issue number50
    DOIs
    Publication statusPublished - 13 Dec 2002

    Cite this