The glycosylation of the variant surface glycoproteins and procyclic acidic repetitive proteins of Trypanosoma brucei

Angela Mehlert, Nicole Zitzmann, Julia M. Richardson, Achim Treumann, Michael A. J. Ferguson

    Research output: Contribution to journalArticlepeer-review

    77 Citations (Scopus)

    Abstract

    Trypanosoma brucei, in common with the other African trypanosomes, exhibits unusual cell-surface molecular architecture, The bloodstream form of the parasite is coated with a continuous layer of approximately five million variant surface glycoprotein (VSG) dimers that provide the parasite with a macromolecular diffusion barrier to guard against lysis by the alternative complement pathway. The procyclic form of the parasite has a more diffuse cell-surface coat made up of approximately 2.5 million copies of procyclic acidic repetitive protein (PARP). Within the VSG and PARP coats exist lower-abundance surface glycoproteins such as receptors and nutrient transporters. Both the VSG molecules and the PARP molecules are attached to the membrane via glycosylphosphatidylinositol (GPI) membrane anchors and the VSGs and one form of PARP are N-glycosylated. In this article, the structures of the N-glycans and the GPI anchors of T. brucei VSGs and PARPs are reviewed and simple models of the surfaces of bloodstream and procyclic trypomastigotes an presented. (C) 1998 Francqui Foundation. Published by Elsevier Science B.V. All rights reserved.

    Original languageEnglish
    Pages (from-to)145-152
    Number of pages8
    JournalMolecular and Biochemical Parasitology
    Volume91
    Issue number1
    DOIs
    Publication statusPublished - 1 Mar 1998

    Keywords

    • Trypanosoma brucei
    • Variant surface glycoprotein
    • Procyclic acidic repetitive protein
    • N-glycosylation
    • Glycosylphosphatidylinositol (GPI)

    Cite this