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Science 25 March 1983:
Vol. 219. no. 4591, pp. 1444 - 1446
DOI: 10.1126/science.6338592

Articles

Science, Vol 219, Issue 4591, 1444-1446
Copyright © 1983 by American Association for the Advancement of Science


articles

A developmentally regulated neuraminidase activity in Trypanosoma cruzi

ME Pereira

The human pathogen Trypanosoma cruzi (Y strain) contains a neuraminidase activity that varies widely in the different developmental stages of the parasite. The specific neuraminidase activity of infective trypomastigotes obtained from tissue culture and from the bloodstream of infected mice is 7 to 15 times higher than that of the acellular culture forms. Amastigotes were devoid of enzyme activity. The enzyme has a pH optimum of 6.0 to 6.5. Live trypanosomes released sialic acid from human erythrocytes and plasma glycoproteins. Several sialyl compounds were hydrolyzed by the parasite, but the best substrate was the protein orosomucoid. Erythrocytes from infected mice with T. cruzi parasitemia were agglutinated by peanut lectin and the hemagglutination titer was correlated with the degree of parasitemia.


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Heterologous Expression of Trypanosoma cruzi trans-Sialidase in Leishmania major Enhances Virulence.
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A Trypanosomal Protein Synergizes with the Cytokines Ciliary Neurotrophic Factor and Leukemia Inhibitory Factor to Prevent Apoptosis of Neuronal Cells.
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The Trypanosoma cruzi trans-Sialidase, through Its Cooh-Terminal Tandem Repeat, Upregulates Interleukin 6 Secretion in Normal Human Intestinal Microvascular Endothelial Cells and Peripheral Blood Mononuclear Cells.
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Gene deletion suggests a role for Trypanosoma cruzi surface glycoprotein GP72 in the insect and mammalian stages of the life cycle.
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Similarity of cruzin, an inhibitor of Trypanosoma cruzi neuraminidase, to high-density lipoprotein.
R. Prioli, J. Ordovas, I Rosenberg, E. Schaefer, and M. Pereira (1987)
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