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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Autores: Izquierdo Lázaro, Luis, Acosta-Serrano, Alvaro, Mehlert, Angela, Ferguson, Michael A. J.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2015
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/99511
Acceso en línea:https://hdl.handle.net/2445/99511
Access Level:acceso abierto
Palabra clave:Malalties parasitàries
Protozoosi
Parasitic diseases
Protozoan diseases
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spelling Identification of a glycosylphosphatidylinositol anchor-modifying beta1-3 galactosyltransferase in Trypanosoma bruceiIzquierdo Lázaro, LuisAcosta-Serrano, AlvaroMehlert, AngelaFerguson, Michael A. J.Malalties parasitàriesProtozoosiParasitic diseasesProtozoan diseasesTrypanosoma 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 Press2016201620152016info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion10 p.application/pdfhttps://hdl.handle.net/2445/99511Articles publicats en revistes (ISGlobal)reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésReproducció del document publicat a: http://dx.doi.org/10.1093/glycob/cwu131Glycobiology, 2015, vol. 25, num. 4, p. 438-447http://dx.doi.org/10.1093/glycob/cwu131cc by (c) Izquierdo et al., 2015http://creativecommons.org/licenses/by/3.0/es/info:eu-repo/semantics/openAccessoai:recercat.cat:2445/995112026-05-29T05:05:01Z
dc.title.none.fl_str_mv Identification of a glycosylphosphatidylinositol anchor-modifying beta1-3 galactosyltransferase in Trypanosoma brucei
title Identification of a glycosylphosphatidylinositol anchor-modifying beta1-3 galactosyltransferase in Trypanosoma brucei
spellingShingle Identification of a glycosylphosphatidylinositol anchor-modifying beta1-3 galactosyltransferase in Trypanosoma brucei
Izquierdo Lázaro, Luis
Malalties parasitàries
Protozoosi
Parasitic diseases
Protozoan diseases
title_short 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_sort Identification of a glycosylphosphatidylinositol anchor-modifying beta1-3 galactosyltransferase in Trypanosoma brucei
dc.creator.none.fl_str_mv Izquierdo Lázaro, Luis
Acosta-Serrano, Alvaro
Mehlert, Angela
Ferguson, Michael A. J.
author Izquierdo Lázaro, Luis
author_facet Izquierdo Lázaro, Luis
Acosta-Serrano, Alvaro
Mehlert, Angela
Ferguson, Michael A. J.
author_role author
author2 Acosta-Serrano, Alvaro
Mehlert, Angela
Ferguson, Michael A. J.
author2_role author
author
author
dc.subject.none.fl_str_mv Malalties parasitàries
Protozoosi
Parasitic diseases
Protozoan diseases
topic Malalties parasitàries
Protozoosi
Parasitic diseases
Protozoan diseases
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.
publishDate 2015
dc.date.none.fl_str_mv 2015
2016
2016
2016
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/99511
url https://hdl.handle.net/2445/99511
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: http://dx.doi.org/10.1093/glycob/cwu131
Glycobiology, 2015, vol. 25, num. 4, p. 438-447
http://dx.doi.org/10.1093/glycob/cwu131
dc.rights.none.fl_str_mv cc by (c) Izquierdo et al., 2015
http://creativecommons.org/licenses/by/3.0/es/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc by (c) Izquierdo et al., 2015
http://creativecommons.org/licenses/by/3.0/es/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 10 p.
application/pdf
dc.publisher.none.fl_str_mv Oxford University Press
publisher.none.fl_str_mv Oxford University Press
dc.source.none.fl_str_mv Articles publicats en revistes (ISGlobal)
reponame:Recercat. Dipósit de la Recerca de Catalunya
instname: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)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
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