The trans-sialidase from Trypanosoma cruzi efficiently transfers α-(2→3)-linked N-glycolylneuraminic acid to terminal β-galactosyl units

The trans-sialidase from Trypanosoma cruzi (TcTS), the agent of Chagas' disease, is a unique enzyme involved in mammalian host-cell invasion. Since T. cruzi is unable to synthesize sialic acids de novo, TcTS catalyzes the transfer of α-(2→3)-sialyl residues from the glycoconjugates of the host...

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Autores principales:	Agustí, R., Giorgi, M.E., de Lederkremer, R.M.
Formato:	JOUR
Materias:	HPAEC Neu5Gc transfer trans-Sialidase Trypanosoma cruzi Antibodies Biosynthesis Carboxylic acids Cells Diseases Mammals Oligosaccharides Chagas disease Galactosyl units Glycolylneuraminic acid Enzyme inhibition galactose n glycoloylneuraminic acid oligosaccharide sialidase anion exchange chromatography article immunomodulation priority journal Animals Galactose Glycoproteins Neuraminic Acids Neuraminidase Mammalia
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_00086215_v342_n16_p2465_Agusti
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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spelling	todo:paper_00086215_v342_n16_p2465_Agusti2023-10-03T14:07:15Z The trans-sialidase from Trypanosoma cruzi efficiently transfers α-(2→3)-linked N-glycolylneuraminic acid to terminal β-galactosyl units Agustí, R. Giorgi, M.E. de Lederkremer, R.M. HPAEC Neu5Gc transfer trans-Sialidase Trypanosoma cruzi Antibodies Biosynthesis Carboxylic acids Cells Diseases Mammals Oligosaccharides Chagas disease Galactosyl units Glycolylneuraminic acid Trypanosoma cruzi Enzyme inhibition galactose n glycoloylneuraminic acid oligosaccharide sialidase anion exchange chromatography article Chagas disease immunomodulation priority journal Trypanosoma cruzi Animals Galactose Glycoproteins Neuraminic Acids Neuraminidase Trypanosoma cruzi Mammalia Trypanosoma cruzi The trans-sialidase from Trypanosoma cruzi (TcTS), the agent of Chagas' disease, is a unique enzyme involved in mammalian host-cell invasion. Since T. cruzi is unable to synthesize sialic acids de novo, TcTS catalyzes the transfer of α-(2→3)-sialyl residues from the glycoconjugates of the host to terminal β-galactopyranosyl units present on the surface of the parasite. TcTS also plays a key role in the immunomodulation of the infected host. Chronic Chagas' disease patients elicit TcTS-neutralizing antibodies that are able to inhibit the enzyme. N-Glycolylneuraminic acid has been detected in T. cruzi, and the trans-sialidase was pointed out as the enzyme involved in its incorporation from host glycoconjugates. However, N-glycolylneuraminic acid α-(2→3)-linked-containing oligosaccharides have not been analyzed as donors in the T. cruzi trans-sialidase reaction. In this paper we studied the ability of TcTS to transfer N-glycolylneuraminic acid from Neu5Gc(α2→3)Gal(β1→4)GlcβOCH2CH2N3 (1) and Neu5Gc(α2→3)Gal(β1→3)GlcNAcβOCH2CH2N3 (2) to lactitol, N-acetyllactosamine and lactose as acceptor substrates. Transfer from 1 was more efficient (50-65%) than from 2 (20-30%) for the three acceptors. The reactions were inhibited when the enzyme was preincubated with a neutralizing antibody. Km values were calculated for 1 and 2 and compared with 3′-sialyllactose using lactitol as acceptor substrate. Analysis was performed by high-performance anion-exchange (HPAEC) chromatography. A competitive transfer reaction of compound 1 in the presence of 3′-sialyllactose and N-acetyllactosamine showed a better transfer of Neu5Gc than of Neu5Ac. © 2007 Elsevier Ltd. All rights reserved. Fil:Agustí, R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Giorgi, M.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:de Lederkremer, R.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00086215_v342_n16_p2465_Agusti
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	HPAEC Neu5Gc transfer trans-Sialidase Trypanosoma cruzi Antibodies Biosynthesis Carboxylic acids Cells Diseases Mammals Oligosaccharides Chagas disease Galactosyl units Glycolylneuraminic acid Trypanosoma cruzi Enzyme inhibition galactose n glycoloylneuraminic acid oligosaccharide sialidase anion exchange chromatography article Chagas disease immunomodulation priority journal Trypanosoma cruzi Animals Galactose Glycoproteins Neuraminic Acids Neuraminidase Trypanosoma cruzi Mammalia Trypanosoma cruzi
spellingShingle	HPAEC Neu5Gc transfer trans-Sialidase Trypanosoma cruzi Antibodies Biosynthesis Carboxylic acids Cells Diseases Mammals Oligosaccharides Chagas disease Galactosyl units Glycolylneuraminic acid Trypanosoma cruzi Enzyme inhibition galactose n glycoloylneuraminic acid oligosaccharide sialidase anion exchange chromatography article Chagas disease immunomodulation priority journal Trypanosoma cruzi Animals Galactose Glycoproteins Neuraminic Acids Neuraminidase Trypanosoma cruzi Mammalia Trypanosoma cruzi Agustí, R. Giorgi, M.E. de Lederkremer, R.M. The trans-sialidase from Trypanosoma cruzi efficiently transfers α-(2→3)-linked N-glycolylneuraminic acid to terminal β-galactosyl units
topic_facet	HPAEC Neu5Gc transfer trans-Sialidase Trypanosoma cruzi Antibodies Biosynthesis Carboxylic acids Cells Diseases Mammals Oligosaccharides Chagas disease Galactosyl units Glycolylneuraminic acid Trypanosoma cruzi Enzyme inhibition galactose n glycoloylneuraminic acid oligosaccharide sialidase anion exchange chromatography article Chagas disease immunomodulation priority journal Trypanosoma cruzi Animals Galactose Glycoproteins Neuraminic Acids Neuraminidase Trypanosoma cruzi Mammalia Trypanosoma cruzi
description	The trans-sialidase from Trypanosoma cruzi (TcTS), the agent of Chagas' disease, is a unique enzyme involved in mammalian host-cell invasion. Since T. cruzi is unable to synthesize sialic acids de novo, TcTS catalyzes the transfer of α-(2→3)-sialyl residues from the glycoconjugates of the host to terminal β-galactopyranosyl units present on the surface of the parasite. TcTS also plays a key role in the immunomodulation of the infected host. Chronic Chagas' disease patients elicit TcTS-neutralizing antibodies that are able to inhibit the enzyme. N-Glycolylneuraminic acid has been detected in T. cruzi, and the trans-sialidase was pointed out as the enzyme involved in its incorporation from host glycoconjugates. However, N-glycolylneuraminic acid α-(2→3)-linked-containing oligosaccharides have not been analyzed as donors in the T. cruzi trans-sialidase reaction. In this paper we studied the ability of TcTS to transfer N-glycolylneuraminic acid from Neu5Gc(α2→3)Gal(β1→4)GlcβOCH2CH2N3 (1) and Neu5Gc(α2→3)Gal(β1→3)GlcNAcβOCH2CH2N3 (2) to lactitol, N-acetyllactosamine and lactose as acceptor substrates. Transfer from 1 was more efficient (50-65%) than from 2 (20-30%) for the three acceptors. The reactions were inhibited when the enzyme was preincubated with a neutralizing antibody. Km values were calculated for 1 and 2 and compared with 3′-sialyllactose using lactitol as acceptor substrate. Analysis was performed by high-performance anion-exchange (HPAEC) chromatography. A competitive transfer reaction of compound 1 in the presence of 3′-sialyllactose and N-acetyllactosamine showed a better transfer of Neu5Gc than of Neu5Ac. © 2007 Elsevier Ltd. All rights reserved.
format	JOUR
author	Agustí, R. Giorgi, M.E. de Lederkremer, R.M.
author_facet	Agustí, R. Giorgi, M.E. de Lederkremer, R.M.
author_sort	Agustí, R.
title	The trans-sialidase from Trypanosoma cruzi efficiently transfers α-(2→3)-linked N-glycolylneuraminic acid to terminal β-galactosyl units
title_short	The trans-sialidase from Trypanosoma cruzi efficiently transfers α-(2→3)-linked N-glycolylneuraminic acid to terminal β-galactosyl units
title_full	The trans-sialidase from Trypanosoma cruzi efficiently transfers α-(2→3)-linked N-glycolylneuraminic acid to terminal β-galactosyl units
title_fullStr	The trans-sialidase from Trypanosoma cruzi efficiently transfers α-(2→3)-linked N-glycolylneuraminic acid to terminal β-galactosyl units
title_full_unstemmed	The trans-sialidase from Trypanosoma cruzi efficiently transfers α-(2→3)-linked N-glycolylneuraminic acid to terminal β-galactosyl units
title_sort	trans-sialidase from trypanosoma cruzi efficiently transfers α-(2→3)-linked n-glycolylneuraminic acid to terminal β-galactosyl units
url	http://hdl.handle.net/20.500.12110/paper_00086215_v342_n16_p2465_Agusti
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_version_	1782028954708738048

The trans-sialidase from Trypanosoma cruzi efficiently transfers α-(2→3)-linked N-glycolylneuraminic acid to terminal β-galactosyl units

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