Selective sialylation of 2,3-di-O-(β-D-galactopyranosyl)-D-galactose catalyzed by Trypanosoma cruzi trans-sialidase
Trypanosoma cruzi, the agent of Chagas' disease, expresses on its surface a trans-sialidase (TcTS) that transfers sialic acid from host glycoconjugates to terminal β-galactopyranosyl units of parasite mucins. This process is involved in infection and pathogenesis. The trisaccharide 2,3-di-O-(β-...
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2005
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09574166_v16_n2_p541_Agusti http://hdl.handle.net/20.500.12110/paper_09574166_v16_n2_p541_Agusti |
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paper:paper_09574166_v16_n2_p541_Agusti2023-06-08T15:56:29Z Selective sialylation of 2,3-di-O-(β-D-galactopyranosyl)-D-galactose catalyzed by Trypanosoma cruzi trans-sialidase 2,3 di o (beta dextro galactopyranosyl) dextro galactose alditol amine galactose glycoside protozoal protein sialic acid sialidase trisaccharide unclassified drug article carbon nuclear magnetic resonance catalysis chemical structure nuclear Overhauser effect priority journal proton nuclear magnetic resonance sialylation Trypanosoma cruzi Trypanosoma cruzi, the agent of Chagas' disease, expresses on its surface a trans-sialidase (TcTS) that transfers sialic acid from host glycoconjugates to terminal β-galactopyranosyl units of parasite mucins. This process is involved in infection and pathogenesis. The trisaccharide 2,3-di-O-(β-d- galactopyranosyl)-d-galactose 1 is an external unit in the larger oligosaccharides of the mucins and a site for sialylation. The trisaccharide was previously synthesized in our laboratory. The last step of the synthesis was the hydrogenolysis of the crystalline benzyl trisaccharide. Herein we prove that the trisaccharide 1, its alditol 3 and the benzyl glycoside 2 are good acceptors of sialic acid and effective inhibitors of the sialylation of N-acetyllactosamine catalyzed by TcTS. Furthermore, selective sialylation of the 1→3 linked galactopyranose in glycoside 2 was determined by one and two-dimensional NMR analysis. In contrast, the flexible 2,3-di-O-(β-d- galactopyranosyl)-d-galactitol 3 is sialylated in either one of the two possible sites. © 2004 Elsevier Ltd. All rights reserved. 2005 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09574166_v16_n2_p541_Agusti http://hdl.handle.net/20.500.12110/paper_09574166_v16_n2_p541_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 |
2,3 di o (beta dextro galactopyranosyl) dextro galactose alditol amine galactose glycoside protozoal protein sialic acid sialidase trisaccharide unclassified drug article carbon nuclear magnetic resonance catalysis chemical structure nuclear Overhauser effect priority journal proton nuclear magnetic resonance sialylation Trypanosoma cruzi |
| spellingShingle |
2,3 di o (beta dextro galactopyranosyl) dextro galactose alditol amine galactose glycoside protozoal protein sialic acid sialidase trisaccharide unclassified drug article carbon nuclear magnetic resonance catalysis chemical structure nuclear Overhauser effect priority journal proton nuclear magnetic resonance sialylation Trypanosoma cruzi Selective sialylation of 2,3-di-O-(β-D-galactopyranosyl)-D-galactose catalyzed by Trypanosoma cruzi trans-sialidase |
| topic_facet |
2,3 di o (beta dextro galactopyranosyl) dextro galactose alditol amine galactose glycoside protozoal protein sialic acid sialidase trisaccharide unclassified drug article carbon nuclear magnetic resonance catalysis chemical structure nuclear Overhauser effect priority journal proton nuclear magnetic resonance sialylation Trypanosoma cruzi |
| description |
Trypanosoma cruzi, the agent of Chagas' disease, expresses on its surface a trans-sialidase (TcTS) that transfers sialic acid from host glycoconjugates to terminal β-galactopyranosyl units of parasite mucins. This process is involved in infection and pathogenesis. The trisaccharide 2,3-di-O-(β-d- galactopyranosyl)-d-galactose 1 is an external unit in the larger oligosaccharides of the mucins and a site for sialylation. The trisaccharide was previously synthesized in our laboratory. The last step of the synthesis was the hydrogenolysis of the crystalline benzyl trisaccharide. Herein we prove that the trisaccharide 1, its alditol 3 and the benzyl glycoside 2 are good acceptors of sialic acid and effective inhibitors of the sialylation of N-acetyllactosamine catalyzed by TcTS. Furthermore, selective sialylation of the 1→3 linked galactopyranose in glycoside 2 was determined by one and two-dimensional NMR analysis. In contrast, the flexible 2,3-di-O-(β-d- galactopyranosyl)-d-galactitol 3 is sialylated in either one of the two possible sites. © 2004 Elsevier Ltd. All rights reserved. |
| title |
Selective sialylation of 2,3-di-O-(β-D-galactopyranosyl)-D-galactose catalyzed by Trypanosoma cruzi trans-sialidase |
| title_short |
Selective sialylation of 2,3-di-O-(β-D-galactopyranosyl)-D-galactose catalyzed by Trypanosoma cruzi trans-sialidase |
| title_full |
Selective sialylation of 2,3-di-O-(β-D-galactopyranosyl)-D-galactose catalyzed by Trypanosoma cruzi trans-sialidase |
| title_fullStr |
Selective sialylation of 2,3-di-O-(β-D-galactopyranosyl)-D-galactose catalyzed by Trypanosoma cruzi trans-sialidase |
| title_full_unstemmed |
Selective sialylation of 2,3-di-O-(β-D-galactopyranosyl)-D-galactose catalyzed by Trypanosoma cruzi trans-sialidase |
| title_sort |
selective sialylation of 2,3-di-o-(β-d-galactopyranosyl)-d-galactose catalyzed by trypanosoma cruzi trans-sialidase |
| publishDate |
2005 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09574166_v16_n2_p541_Agusti http://hdl.handle.net/20.500.12110/paper_09574166_v16_n2_p541_Agusti |
| _version_ |
1768544740951719936 |