Journal
GLYCOBIOLOGY
Volume 25, Issue 4, Pages 438-447Publisher
OXFORD UNIV PRESS INC
DOI: 10.1093/glycob/cwu131
Keywords
galactosyltransferase; GPI-anchor; procyclic form; TbGT3; Trypanosoma brucei
Categories
Funding
- Wellcome Trust [101842, WT093691MA, 097945]
- Ramon y Cajal Program (Spanish Ministry of Economy and Competitiveness)
- GlycoPar-EU
Ask authors/readers for more resources
Trypanosoma brucei is the causative agent of human African sleeping sickness and the cattle disease nagana. Trypanosoma brucei is dependent on glycoproteins for its survival and infectivity throughout its life cycle. Here we report the functional characterization of TbGT3, a glycosyltransferase expressed in the bloodstream and procyclic form of the parasite. Bloodstream and procyclic form TbGT3 conditional null mutants were created and both exhibited normal growth under permissive and nonpermissive conditions. Under nonpermissive conditions, the normal glycosylation of the major glycoprotein of bloodstream form T. brucei, the variant surface glycoprotein and the absence of major alterations in lectin binding to other glycoproteins suggested that the major function of TbGT3 occurs in the procyclic form of the parasite. Consistent with this, the major surface glycoprotein of the procyclic form, procyclin, exhibited a marked reduction in molecular weight due to changes in glycosylphosphatidylinositol (GPI) anchor side chains. Structural analysis of the mutant procyclin GPI anchors indicated that TbGT3 encodes a UDP-Gal: beta-GlcNAc-GPI beta 1-3 Gal transferase. Despite the alterations in GPI anchor side chains, TbGT3 conditional null mutants remained infectious to tsetse flies under nonpermissive conditions.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available