Trans-sialidase and mucins of Trypanosoma cruzi: An important interplay for the parasite
A dense glycocalix covers the surface of Trypanosoma cruzi, the agent of Chagas disease. Sialic acid in the surface of the parasite plays an important role in the infectious process, however, T. cruzi is unable to synthesize sialic acid or the usual donor CMP-sialic acid. Instead, T. cruzi expresses...
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2011
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00086215_v346_n12_p1389_EugeniaGiorgi http://hdl.handle.net/20.500.12110/paper_00086215_v346_n12_p1389_EugeniaGiorgi |
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paper:paper_00086215_v346_n12_p1389_EugeniaGiorgi2023-06-08T14:32:58Z Trans-sialidase and mucins of Trypanosoma cruzi: An important interplay for the parasite Chagas disease Mucins Trans-sialidase Trypanosoma cruzi Chagas disease Epimastigotes Glycoconjugates Glycosylphosphatidylinositol anchors Immune systems Mucins Parasite- Sialic acids Trans-sialidases Trypanosoma cruzi Cell membranes Sugars Carboxylic acids glycoconjugate glycosylphosphatidylinositol mucin oligosaccharide sialidase article carbohydrate analysis enzyme activity epimastigote nonhuman priority journal sialylation Trypanosoma cruzi trypomastigote Animals Carbohydrate Sequence Chagas Disease Enzyme Inhibitors Glycoconjugates Glycoproteins Glycosylphosphatidylinositols Humans Life Cycle Stages Molecular Sequence Data Mucins Neuraminidase Protein Binding Sialic Acids Species Specificity Trypanosoma cruzi Type C Phospholipases Hexapoda Mammalia Trypanosoma cruzi A dense glycocalix covers the surface of Trypanosoma cruzi, the agent of Chagas disease. Sialic acid in the surface of the parasite plays an important role in the infectious process, however, T. cruzi is unable to synthesize sialic acid or the usual donor CMP-sialic acid. Instead, T. cruzi expresses a unique enzyme, the trans-sialidase (TcTS) involved in the transfer of sialic acid from host glycoconjugates to mucins of the parasite. The mucins are the major glycoproteins in the insect stage epimastigotes and in the infective trypomastigotes. Both, the mucins and the TcTS are anchored to the plasma membrane by a glycosylphosphatidylinositol anchor. Thus, TcTS may be shed into the bloodstream of the mammal host by the action of a parasite phosphatidylinositol-phospholipase C, affecting the immune system. The composition and structure of the sugars in the parasite mucins is characteristic of each differentiation stage, also, interstrain variations were described for epimastigote mucins. This review focus on the characteristics of the interplay between the trans-sialidase and the mucins of T. cruzi and summarizes the known carbohydrate structures of the mucins. © 2011 Elsevier Ltd. All rights reserved. 2011 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00086215_v346_n12_p1389_EugeniaGiorgi http://hdl.handle.net/20.500.12110/paper_00086215_v346_n12_p1389_EugeniaGiorgi |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Chagas disease Mucins Trans-sialidase Trypanosoma cruzi Chagas disease Epimastigotes Glycoconjugates Glycosylphosphatidylinositol anchors Immune systems Mucins Parasite- Sialic acids Trans-sialidases Trypanosoma cruzi Cell membranes Sugars Carboxylic acids glycoconjugate glycosylphosphatidylinositol mucin oligosaccharide sialidase article carbohydrate analysis enzyme activity epimastigote nonhuman priority journal sialylation Trypanosoma cruzi trypomastigote Animals Carbohydrate Sequence Chagas Disease Enzyme Inhibitors Glycoconjugates Glycoproteins Glycosylphosphatidylinositols Humans Life Cycle Stages Molecular Sequence Data Mucins Neuraminidase Protein Binding Sialic Acids Species Specificity Trypanosoma cruzi Type C Phospholipases Hexapoda Mammalia Trypanosoma cruzi |
| spellingShingle |
Chagas disease Mucins Trans-sialidase Trypanosoma cruzi Chagas disease Epimastigotes Glycoconjugates Glycosylphosphatidylinositol anchors Immune systems Mucins Parasite- Sialic acids Trans-sialidases Trypanosoma cruzi Cell membranes Sugars Carboxylic acids glycoconjugate glycosylphosphatidylinositol mucin oligosaccharide sialidase article carbohydrate analysis enzyme activity epimastigote nonhuman priority journal sialylation Trypanosoma cruzi trypomastigote Animals Carbohydrate Sequence Chagas Disease Enzyme Inhibitors Glycoconjugates Glycoproteins Glycosylphosphatidylinositols Humans Life Cycle Stages Molecular Sequence Data Mucins Neuraminidase Protein Binding Sialic Acids Species Specificity Trypanosoma cruzi Type C Phospholipases Hexapoda Mammalia Trypanosoma cruzi Trans-sialidase and mucins of Trypanosoma cruzi: An important interplay for the parasite |
| topic_facet |
Chagas disease Mucins Trans-sialidase Trypanosoma cruzi Chagas disease Epimastigotes Glycoconjugates Glycosylphosphatidylinositol anchors Immune systems Mucins Parasite- Sialic acids Trans-sialidases Trypanosoma cruzi Cell membranes Sugars Carboxylic acids glycoconjugate glycosylphosphatidylinositol mucin oligosaccharide sialidase article carbohydrate analysis enzyme activity epimastigote nonhuman priority journal sialylation Trypanosoma cruzi trypomastigote Animals Carbohydrate Sequence Chagas Disease Enzyme Inhibitors Glycoconjugates Glycoproteins Glycosylphosphatidylinositols Humans Life Cycle Stages Molecular Sequence Data Mucins Neuraminidase Protein Binding Sialic Acids Species Specificity Trypanosoma cruzi Type C Phospholipases Hexapoda Mammalia Trypanosoma cruzi |
| description |
A dense glycocalix covers the surface of Trypanosoma cruzi, the agent of Chagas disease. Sialic acid in the surface of the parasite plays an important role in the infectious process, however, T. cruzi is unable to synthesize sialic acid or the usual donor CMP-sialic acid. Instead, T. cruzi expresses a unique enzyme, the trans-sialidase (TcTS) involved in the transfer of sialic acid from host glycoconjugates to mucins of the parasite. The mucins are the major glycoproteins in the insect stage epimastigotes and in the infective trypomastigotes. Both, the mucins and the TcTS are anchored to the plasma membrane by a glycosylphosphatidylinositol anchor. Thus, TcTS may be shed into the bloodstream of the mammal host by the action of a parasite phosphatidylinositol-phospholipase C, affecting the immune system. The composition and structure of the sugars in the parasite mucins is characteristic of each differentiation stage, also, interstrain variations were described for epimastigote mucins. This review focus on the characteristics of the interplay between the trans-sialidase and the mucins of T. cruzi and summarizes the known carbohydrate structures of the mucins. © 2011 Elsevier Ltd. All rights reserved. |
| title |
Trans-sialidase and mucins of Trypanosoma cruzi: An important interplay for the parasite |
| title_short |
Trans-sialidase and mucins of Trypanosoma cruzi: An important interplay for the parasite |
| title_full |
Trans-sialidase and mucins of Trypanosoma cruzi: An important interplay for the parasite |
| title_fullStr |
Trans-sialidase and mucins of Trypanosoma cruzi: An important interplay for the parasite |
| title_full_unstemmed |
Trans-sialidase and mucins of Trypanosoma cruzi: An important interplay for the parasite |
| title_sort |
trans-sialidase and mucins of trypanosoma cruzi: an important interplay for the parasite |
| publishDate |
2011 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00086215_v346_n12_p1389_EugeniaGiorgi http://hdl.handle.net/20.500.12110/paper_00086215_v346_n12_p1389_EugeniaGiorgi |
| _version_ |
1768542531612573696 |