Literature DB >> 15463763

Trypanosoma cruzi trans-sialidase and cell invasion.

S Schenkman1, D Eichinger.   

Abstract

Trypanosoma cruzi does not synthesize sialic acid but does contain a trans-sialidase, an enzyme capable of transferring sialic acid between host glycoconjugates and the parasite. Sialic acids are negatively charged carbohydrates attached to the terminal non-reducing end of glycoproteins and glycolipids, and their presence can dramatically influence many cell-surface recognition processes. Since sialic acids have been implicated in several ligand-receptor interactions, including the interaction of pathogenic viruses, bacteria and protozoans with their hosts, the expression of trans-sialidase and the acquisition of sialic acid by T. cruzi may be relevant to the interaction of the parasite with the host, and consequently may influence the pathobiology of Chagas disease. In this review, Sergio Schenkman and Daniel Eichinger discuss recent data about the structure and function of T. cruzi trans-sialidase.

Entities:  

Year:  1993        PMID: 15463763     DOI: 10.1016/0169-4758(93)90017-a

Source DB:  PubMed          Journal:  Parasitol Today        ISSN: 0169-4758


  24 in total

1.  Epitope mapping of trans-sialidase from Trypanosoma cruzi reveals the presence of several cross-reactive determinants.

Authors:  T A Pitcovsky; J Mucci; P Alvarez; M S Leguizamón; O Burrone; P M Alzari; O Campetella
Journal:  Infect Immun       Date:  2001-03       Impact factor: 3.441

2.  The major surface glycoprotein of Trypanosoma cruzi amastigotes are ligands of the human serum mannose-binding protein.

Authors:  S J Kahn; M Wleklinski; R A Ezekowitz; D Coder; A Aruffo; A Farr
Journal:  Infect Immun       Date:  1996-07       Impact factor: 3.441

3.  Differential expression and characterization of a member of the mucin-associated surface protein family secreted by Trypanosoma cruzi.

Authors:  Luis Miguel De Pablos; Gloria González González; Jennifer Solano Parada; Víctor Seco Hidalgo; Isabel María Díaz Lozano; María Mercedes Gómez Samblás; Teresa Cruz Bustos; Antonio Osuna
Journal:  Infect Immun       Date:  2011-07-25       Impact factor: 3.441

4.  Galactosyl-lactose sialylation using Trypanosoma cruzi trans-sialidase as the biocatalyst and bovine κ-casein-derived glycomacropeptide as the donor substrate.

Authors:  Maarten H Wilbrink; Geert A ten Kate; Sander S van Leeuwen; Peter Sanders; Erik Sallomons; Johannes A Hage; Lubbert Dijkhuizen; Johannis P Kamerling
Journal:  Appl Environ Microbiol       Date:  2014-07-25       Impact factor: 4.792

Review 5.  The potential role of sialoadhesin as a macrophage recognition molecule in health and disease.

Authors:  P R Crocker; A Hartnell; J Munday; D Nath
Journal:  Glycoconj J       Date:  1997-08       Impact factor: 2.916

6.  Role of host lysosomal associated membrane protein (LAMP) in Trypanosoma cruzi invasion and intracellular development.

Authors:  L A G Albertti; A M Macedo; E Chiari; N W Andrews; L O Andrade
Journal:  Microbes Infect       Date:  2010-06-16       Impact factor: 2.700

7.  Trans-sialidase Protein as a Potential Serological Marker for African Trypanosomiasis.

Authors:  Ana Filipa Teixeira; João Gomes Pereira; Sónia Pestana-Ascensão; Marcelo Sousa Silva
Journal:  Protein J       Date:  2019-02       Impact factor: 2.371

8.  Trypanosoma cruzi amastigote adhesion to macrophages is facilitated by the mannose receptor.

Authors:  S Kahn; M Wleklinski; A Aruffo; A Farr; D Coder; M Kahn
Journal:  J Exp Med       Date:  1995-11-01       Impact factor: 14.307

9.  Ecto-ATPase activity on the surface of Trypanosoma cruzi and its possible role in the parasite-host cell interaction.

Authors:  Danielle F R Bisaggio; Carlos Eduardo Peres-Sampaio; José Roberto Meyer-Fernandes; Thaïs Souto-Padrón
Journal:  Parasitol Res       Date:  2003-08-22       Impact factor: 2.289

10.  Flagellum-mediated adhesion of Trypanosoma congolense to bovine aorta endothelial cells.

Authors:  A Hemphill; C A Ross
Journal:  Parasitol Res       Date:  1995       Impact factor: 2.289

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