Identification of a glycosylphosphatidylinositol anchor-modifying beta1-3 galactosyltransferase in Trypanosoma brucei

Trypanosoma brucei is the causative agent of human African sleeping sickness and the cattle disease nagana. T. 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...

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Authors: Izquierdo Lázaro, Luis; Acosta-Serrano, Alvaro; Mehlert, Angela; Ferguson, Michael A. J.
Format: Article
Status:Published version
Publication date:2015
Country:España
Institution:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repository:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/99511
Online Access:https://hdl.handle.net/2445/99511
Access Level:Open access
Keyword:Malalties parasitàries
Protozoosi
Parasitic diseases
Protozoan diseases
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author Izquierdo Lázaro, Luis
author2 Acosta-Serrano, Alvaro
Mehlert, Angela
Ferguson, Michael A. J.
author2_role author
author
author
author_browse Acosta-Serrano, Alvaro
Ferguson, Michael A. J.
Izquierdo Lázaro, Luis
Mehlert, Angela
author_facet Izquierdo Lázaro, Luis
Acosta-Serrano, Alvaro
Mehlert, Angela
Ferguson, Michael A. J.
author_role author
collection Recercat. Dipósit de la Recerca de Catalunya
description Trypanosoma brucei is the causative agent of human African sleeping sickness and the cattle disease nagana. T. 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 non-permissive conditions. Under non-permissive 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 beta1-3 Gal transferase. Despite the alterations in GPI anchor side chains, TbGT3 conditional null mutants remained infectious to tsetse flies under non-permissive conditions.
eu_rights_str_mv openAccess
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institution Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
network_acronym_str ES
network_name_str España
oai_identifier_str oai:recercat.cat:2445/99511
publishDate 2015
publishDateSort 2015
publisher Oxford University Press
publisherStr Oxford University Press
reponame_str Recercat. Dipósit de la Recerca de Catalunya
spelling Identification of a glycosylphosphatidylinositol anchor-modifying beta1-3 galactosyltransferase in Trypanosoma brucei Izquierdo Lázaro, Luis Acosta-Serrano, Alvaro Mehlert, Angela Ferguson, Michael A. J. Malalties parasitàries Protozoosi Parasitic diseases Protozoan diseases Trypanosoma brucei is the causative agent of human African sleeping sickness and the cattle disease nagana. T. 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 non-permissive conditions. Under non-permissive 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 beta1-3 Gal transferase. Despite the alterations in GPI anchor side chains, TbGT3 conditional null mutants remained infectious to tsetse flies under non-permissive conditions. Oxford University Press https://hdl.handle.net/2445/99511
spellingShingle Identification of a glycosylphosphatidylinositol anchor-modifying beta1-3 galactosyltransferase in Trypanosoma brucei
Izquierdo Lázaro, Luis
Malalties parasitàries
Protozoosi
Parasitic diseases
Protozoan diseases
status_str publishedVersion
title Identification of a glycosylphosphatidylinositol anchor-modifying beta1-3 galactosyltransferase in Trypanosoma brucei
title_full Identification of a glycosylphosphatidylinositol anchor-modifying beta1-3 galactosyltransferase in Trypanosoma brucei
title_fullStr Identification of a glycosylphosphatidylinositol anchor-modifying beta1-3 galactosyltransferase in Trypanosoma brucei
title_full_unstemmed Identification of a glycosylphosphatidylinositol anchor-modifying beta1-3 galactosyltransferase in Trypanosoma brucei
title_short Identification of a glycosylphosphatidylinositol anchor-modifying beta1-3 galactosyltransferase in Trypanosoma brucei
title_sort Identification of a glycosylphosphatidylinositol anchor-modifying beta1-3 galactosyltransferase in Trypanosoma brucei
topic Malalties parasitàries
Protozoosi
Parasitic diseases
Protozoan diseases
topic_facet Malalties parasitàries
Protozoosi
Parasitic diseases
Protozoan diseases
url https://hdl.handle.net/2445/99511