Comparative rates of sialylation by recombinant trans-sialidase and inhibitor properties of synthetic oligosaccharides from Trypanosoma cruzi mucins-containing galactofuranose and galactopyranose
The mucin-like glycoproteins of Trypanosoma cruzi have novel O-linked oligosaccharides that are acceptors of sialic acid in the trans-sialidase (TcTS) reaction. The transference of sialic acid from host glycoconjugates to the mucins is involved in infection and pathogenesis. The O-linked chains may...
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todo:paper_09680896_v15_n7_p2611_Agusti2023-10-03T15:55:11Z Comparative rates of sialylation by recombinant trans-sialidase and inhibitor properties of synthetic oligosaccharides from Trypanosoma cruzi mucins-containing galactofuranose and galactopyranose Agustí, R. Giorgi, M.E. Mendoza, V.M. Gallo-Rodriguez, C. de Lederkremer, R.M. Galactofuranose HPAEC-PAD Mucins trans-Sialidase Trypanosoma cruzi alditol amine benzyl glycoside carbohydrate derivative galactofuranose galactopyranose glycoside lactose monosaccharide mucin n acetyllactosamine oligosaccharide recombinant enzyme sialic acid sialidase sialyllactose sugar unclassified drug article carbohydrate synthesis comparative study drug synthesis enzyme mechanism enzyme substrate IC 50 nonhuman parasite virulence protozoal infection sialylation strain identification structure activity relation transport kinetics Trypanosoma cruzi Amino Sugars Animals Carbohydrate Sequence Escherichia coli Galactose Kinetics Molecular Sequence Data Mucins Neuraminidase Oligosaccharides Recombinant Proteins Sialic Acids Trypanosoma cruzi Trypanosoma cruzi The mucin-like glycoproteins of Trypanosoma cruzi have novel O-linked oligosaccharides that are acceptors of sialic acid in the trans-sialidase (TcTS) reaction. The transference of sialic acid from host glycoconjugates to the mucins is involved in infection and pathogenesis. The O-linked chains may contain galactofuranose in addition to the acceptor galactopyranose units. Thus far, the galactofuranose form was found in the mucins of strains belonging to the less infective lineage. The acceptor properties of the chemically synthesized oligosaccharides were now studied in order to correlate their structure with the ability to act as substrates. Recombinant TcTS and sialyllactose as donor were used. The reactions were followed by HPAEC-PAD. The Km values were calculated for the free sugars, the sugar alditols and the benzyl glycosides. All the compounds showed to be good acceptors of sialic acid. Thus, the introduction of galactofuranose in the mucins of the strains of lineage 1 would not be responsible for the diminished virulence of the strains. The oligosaccharides and derivatives inhibited the transfer of sialic acid to the substrate N-acetyllactosamine with IC50 values between 0.6 and 4 mM. © 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:Mendoza, V.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Gallo-Rodriguez, C. 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_09680896_v15_n7_p2611_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 |
Galactofuranose HPAEC-PAD Mucins trans-Sialidase Trypanosoma cruzi alditol amine benzyl glycoside carbohydrate derivative galactofuranose galactopyranose glycoside lactose monosaccharide mucin n acetyllactosamine oligosaccharide recombinant enzyme sialic acid sialidase sialyllactose sugar unclassified drug article carbohydrate synthesis comparative study drug synthesis enzyme mechanism enzyme substrate IC 50 nonhuman parasite virulence protozoal infection sialylation strain identification structure activity relation transport kinetics Trypanosoma cruzi Amino Sugars Animals Carbohydrate Sequence Escherichia coli Galactose Kinetics Molecular Sequence Data Mucins Neuraminidase Oligosaccharides Recombinant Proteins Sialic Acids Trypanosoma cruzi Trypanosoma cruzi |
spellingShingle |
Galactofuranose HPAEC-PAD Mucins trans-Sialidase Trypanosoma cruzi alditol amine benzyl glycoside carbohydrate derivative galactofuranose galactopyranose glycoside lactose monosaccharide mucin n acetyllactosamine oligosaccharide recombinant enzyme sialic acid sialidase sialyllactose sugar unclassified drug article carbohydrate synthesis comparative study drug synthesis enzyme mechanism enzyme substrate IC 50 nonhuman parasite virulence protozoal infection sialylation strain identification structure activity relation transport kinetics Trypanosoma cruzi Amino Sugars Animals Carbohydrate Sequence Escherichia coli Galactose Kinetics Molecular Sequence Data Mucins Neuraminidase Oligosaccharides Recombinant Proteins Sialic Acids Trypanosoma cruzi Trypanosoma cruzi Agustí, R. Giorgi, M.E. Mendoza, V.M. Gallo-Rodriguez, C. de Lederkremer, R.M. Comparative rates of sialylation by recombinant trans-sialidase and inhibitor properties of synthetic oligosaccharides from Trypanosoma cruzi mucins-containing galactofuranose and galactopyranose |
topic_facet |
Galactofuranose HPAEC-PAD Mucins trans-Sialidase Trypanosoma cruzi alditol amine benzyl glycoside carbohydrate derivative galactofuranose galactopyranose glycoside lactose monosaccharide mucin n acetyllactosamine oligosaccharide recombinant enzyme sialic acid sialidase sialyllactose sugar unclassified drug article carbohydrate synthesis comparative study drug synthesis enzyme mechanism enzyme substrate IC 50 nonhuman parasite virulence protozoal infection sialylation strain identification structure activity relation transport kinetics Trypanosoma cruzi Amino Sugars Animals Carbohydrate Sequence Escherichia coli Galactose Kinetics Molecular Sequence Data Mucins Neuraminidase Oligosaccharides Recombinant Proteins Sialic Acids Trypanosoma cruzi Trypanosoma cruzi |
description |
The mucin-like glycoproteins of Trypanosoma cruzi have novel O-linked oligosaccharides that are acceptors of sialic acid in the trans-sialidase (TcTS) reaction. The transference of sialic acid from host glycoconjugates to the mucins is involved in infection and pathogenesis. The O-linked chains may contain galactofuranose in addition to the acceptor galactopyranose units. Thus far, the galactofuranose form was found in the mucins of strains belonging to the less infective lineage. The acceptor properties of the chemically synthesized oligosaccharides were now studied in order to correlate their structure with the ability to act as substrates. Recombinant TcTS and sialyllactose as donor were used. The reactions were followed by HPAEC-PAD. The Km values were calculated for the free sugars, the sugar alditols and the benzyl glycosides. All the compounds showed to be good acceptors of sialic acid. Thus, the introduction of galactofuranose in the mucins of the strains of lineage 1 would not be responsible for the diminished virulence of the strains. The oligosaccharides and derivatives inhibited the transfer of sialic acid to the substrate N-acetyllactosamine with IC50 values between 0.6 and 4 mM. © 2007 Elsevier Ltd. All rights reserved. |
format |
JOUR |
author |
Agustí, R. Giorgi, M.E. Mendoza, V.M. Gallo-Rodriguez, C. de Lederkremer, R.M. |
author_facet |
Agustí, R. Giorgi, M.E. Mendoza, V.M. Gallo-Rodriguez, C. de Lederkremer, R.M. |
author_sort |
Agustí, R. |
title |
Comparative rates of sialylation by recombinant trans-sialidase and inhibitor properties of synthetic oligosaccharides from Trypanosoma cruzi mucins-containing galactofuranose and galactopyranose |
title_short |
Comparative rates of sialylation by recombinant trans-sialidase and inhibitor properties of synthetic oligosaccharides from Trypanosoma cruzi mucins-containing galactofuranose and galactopyranose |
title_full |
Comparative rates of sialylation by recombinant trans-sialidase and inhibitor properties of synthetic oligosaccharides from Trypanosoma cruzi mucins-containing galactofuranose and galactopyranose |
title_fullStr |
Comparative rates of sialylation by recombinant trans-sialidase and inhibitor properties of synthetic oligosaccharides from Trypanosoma cruzi mucins-containing galactofuranose and galactopyranose |
title_full_unstemmed |
Comparative rates of sialylation by recombinant trans-sialidase and inhibitor properties of synthetic oligosaccharides from Trypanosoma cruzi mucins-containing galactofuranose and galactopyranose |
title_sort |
comparative rates of sialylation by recombinant trans-sialidase and inhibitor properties of synthetic oligosaccharides from trypanosoma cruzi mucins-containing galactofuranose and galactopyranose |
url |
http://hdl.handle.net/20.500.12110/paper_09680896_v15_n7_p2611_Agusti |
work_keys_str_mv |
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