1. Cloning, localization and differential expression of the Trypanosoma cruzi TcOGNT-2 glycosyl transferase
- Author
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Carlos Robello, Adriana Parodi-Talice, Eduardo Osinaga, María Laura Chiribao, María Gabriela Libisch, Institut Pasteur de Montevideo, Réseau International des Instituts Pasteur (RIIP), Departamento de Bioquimica, Facultad de Medicina- Universidad de la República [Montevideo] (UCUR), Departamento de inmunobiologia, Seccion Genetica, Facultad de Ciencias- Universidad de la República [Montevideo] (UCUR), This work was supported by grants from the 'Agencia Nacional de Investigación e Innovación' ANII (FCE2007_357) and a research fellowship from the ANII (MLC). A.P.T., E.O. and C.R. are researchers from the Sistema Nacional de Investigadores (ANII), Montevideo, Uruguay., and Universidad de la República [Montevideo] (UCUR)-Facultad de Ciencias
- Subjects
Chagas disease ,Trypanosoma cruzi ,Glycosyl-transferase ,Golgi Apparatus ,Neuraminidase ,Biology ,Gene Expression Regulation, Enzymologic ,Uridine Diphosphate ,Acetylglucosamine ,Serine ,03 medical and health sciences ,symbols.namesake ,Differential expression ,Chlorocebus aethiops ,Glycosyltransferase ,Genetics ,Animals ,Cloning, Molecular ,Threonine ,3' Untranslated Regions ,Vero Cells ,Gene ,Glycoproteins ,030304 developmental biology ,O-glycosylation ,chemistry.chemical_classification ,Life Cycle Stages ,0303 health sciences ,030302 biochemistry & molecular biology ,Mucin ,Glycosyltransferases ,General Medicine ,Golgi apparatus ,biology.organism_classification ,carbohydrates (lipids) ,[SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology ,Enzyme ,Infectivity ,chemistry ,Biochemistry ,biology.protein ,symbols ,Rabbits - Abstract
International audience; The surface of Trypanosoma cruzi is covered by a dense glycocalix which is characteristic of each stage of the life cycle. Its composition and complexity depend mainly on mucin-like proteins. A remarkable feature of O-glycan biosynthesis in trypanosomes is that it initiates with the addition of a GlcNAc instead of the GalNAc residue that is commonly used in vertebrate mucins. The fact that the interplay between trans-sialidase and mucin is crucial for pathogenesis, and both families have stage-specific members is also remarkable. Recently the enzyme that transfers the first GlcNAc from UDP-GlcNAc to a serine or threonine residue was kinetically characterized. The relevance of this enzyme is evidenced by its role as catalyzer of the first step in O-glycosylation. In this paper we describe how this gene is expressed differentially along the life cycle with a pattern that is very similar to that of trans-sialidases. Its localization was determined, showing that the protein predicted to be in the Golgi apparatus is also present in reservosomes. Finally our results indicate that this enzyme, when overexpressed, enhances T. cruzi infectivity.
- Published
- 2012