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

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 mac...

Full description

Bibliographic Details
Main Authors: Mehlert, A, Zitzmann, N, Richardson, J, Treumann, A, Ferguson, M
Format: Journal article
Language:English
Published: Elsevier 1998
_version_ 1826278049146994688
author Mehlert, A
Zitzmann, N
Richardson, J
Treumann, A
Ferguson, M
author_facet Mehlert, A
Zitzmann, N
Richardson, J
Treumann, A
Ferguson, M
author_sort Mehlert, A
collection OXFORD
description 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 are presented.
first_indexed 2024-03-06T23:38:07Z
format Journal article
id oxford-uuid:6e5d3e19-bb11-480e-852e-957525bc8b2a
institution University of Oxford
language English
last_indexed 2024-03-06T23:38:07Z
publishDate 1998
publisher Elsevier
record_format dspace
spelling oxford-uuid:6e5d3e19-bb11-480e-852e-957525bc8b2a2022-03-26T19:24:00ZThe glycosylation of the variant surface glycoproteins and procyclic acidic repetitive proteins of Trypanosoma bruceiJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:6e5d3e19-bb11-480e-852e-957525bc8b2aEnglishSymplectic Elements at OxfordElsevier1998Mehlert, AZitzmann, NRichardson, JTreumann, AFerguson, MTrypanosoma 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 are presented.
spellingShingle Mehlert, A
Zitzmann, N
Richardson, J
Treumann, A
Ferguson, M
The glycosylation of the variant surface glycoproteins and procyclic acidic repetitive proteins of Trypanosoma brucei
title The glycosylation of the variant surface glycoproteins and procyclic acidic repetitive proteins of Trypanosoma brucei
title_full The glycosylation of the variant surface glycoproteins and procyclic acidic repetitive proteins of Trypanosoma brucei
title_fullStr The glycosylation of the variant surface glycoproteins and procyclic acidic repetitive proteins of Trypanosoma brucei
title_full_unstemmed The glycosylation of the variant surface glycoproteins and procyclic acidic repetitive proteins of Trypanosoma brucei
title_short The glycosylation of the variant surface glycoproteins and procyclic acidic repetitive proteins of Trypanosoma brucei
title_sort glycosylation of the variant surface glycoproteins and procyclic acidic repetitive proteins of trypanosoma brucei
work_keys_str_mv AT mehlerta theglycosylationofthevariantsurfaceglycoproteinsandprocyclicacidicrepetitiveproteinsoftrypanosomabrucei
AT zitzmannn theglycosylationofthevariantsurfaceglycoproteinsandprocyclicacidicrepetitiveproteinsoftrypanosomabrucei
AT richardsonj theglycosylationofthevariantsurfaceglycoproteinsandprocyclicacidicrepetitiveproteinsoftrypanosomabrucei
AT treumanna theglycosylationofthevariantsurfaceglycoproteinsandprocyclicacidicrepetitiveproteinsoftrypanosomabrucei
AT fergusonm theglycosylationofthevariantsurfaceglycoproteinsandprocyclicacidicrepetitiveproteinsoftrypanosomabrucei
AT mehlerta glycosylationofthevariantsurfaceglycoproteinsandprocyclicacidicrepetitiveproteinsoftrypanosomabrucei
AT zitzmannn glycosylationofthevariantsurfaceglycoproteinsandprocyclicacidicrepetitiveproteinsoftrypanosomabrucei
AT richardsonj glycosylationofthevariantsurfaceglycoproteinsandprocyclicacidicrepetitiveproteinsoftrypanosomabrucei
AT treumanna glycosylationofthevariantsurfaceglycoproteinsandprocyclicacidicrepetitiveproteinsoftrypanosomabrucei
AT fergusonm glycosylationofthevariantsurfaceglycoproteinsandprocyclicacidicrepetitiveproteinsoftrypanosomabrucei