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Abstract:

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.

Registro:

Documento: Artículo
Título:Trans-sialidase and mucins of Trypanosoma cruzi: An important interplay for the parasite
Autor:Eugenia Giorgi, M.; De Lederkremer, R.M.
Filiación:CIHIDECAR, Departamento de Química Orgánica, Ciudad Universitaria, Pabellón II, 1428 Buenos Aires, Argentina
Palabras clave: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
Año:2011
Volumen:346
Número:12
Página de inicio:1389
Página de fin:1393
DOI: http://dx.doi.org/10.1016/j.carres.2011.04.006
Título revista:Carbohydrate Research
Título revista abreviado:Carbohydr. Res.
ISSN:00086215
CODEN:CRBRA
CAS:sialidase, 9001-67-6; Enzyme Inhibitors; Glycoconjugates; Glycoproteins; Glycosylphosphatidylinositols; Mucins; Neuraminidase, 3.2.1.18; Sialic Acids; Type C Phospholipases, 3.1.4.-; trans-sialidase, 3.2.1.-
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00086215_v346_n12_p1389_EugeniaGiorgi

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Citas:

---------- APA ----------
Eugenia Giorgi, M. & De Lederkremer, R.M. (2011) . Trans-sialidase and mucins of Trypanosoma cruzi: An important interplay for the parasite. Carbohydrate Research, 346(12), 1389-1393.
http://dx.doi.org/10.1016/j.carres.2011.04.006
---------- CHICAGO ----------
Eugenia Giorgi, M., De Lederkremer, R.M. "Trans-sialidase and mucins of Trypanosoma cruzi: An important interplay for the parasite" . Carbohydrate Research 346, no. 12 (2011) : 1389-1393.
http://dx.doi.org/10.1016/j.carres.2011.04.006
---------- MLA ----------
Eugenia Giorgi, M., De Lederkremer, R.M. "Trans-sialidase and mucins of Trypanosoma cruzi: An important interplay for the parasite" . Carbohydrate Research, vol. 346, no. 12, 2011, pp. 1389-1393.
http://dx.doi.org/10.1016/j.carres.2011.04.006
---------- VANCOUVER ----------
Eugenia Giorgi, M., De Lederkremer, R.M. Trans-sialidase and mucins of Trypanosoma cruzi: An important interplay for the parasite. Carbohydr. Res. 2011;346(12):1389-1393.
http://dx.doi.org/10.1016/j.carres.2011.04.006