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Trypanosoma cruzi trans-sialidase and neuraminidase activities can be mediated by the same enzymes

Trans-sialidase and neuraminidase activities have been detected on the surface membrane of trypomastigotes of Trypanosoma cruzi, and both have been implicated in the parasite's invasion of host cells. We show here that these enzymes are structurally related. They are recognized by two independe...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1992
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2119131/
https://www.ncbi.nlm.nih.gov/pubmed/1732417
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description Trans-sialidase and neuraminidase activities have been detected on the surface membrane of trypomastigotes of Trypanosoma cruzi, and both have been implicated in the parasite's invasion of host cells. We show here that these enzymes are structurally related. They are recognized by two independently derived monoclonal antibodies, are anchored to the membrane by glycosylphosphatidylinositol, copurify by ion exchange, molecular sieving, and hydrophobic chromatography, have maximal activities between pH 6.5 and 7.5, and are inactivated by heating at 56 degrees C. Furthermore, the neuraminidase and trans-sialidase reactions are coupled. An increase of the concentration of acceptors of the transfer reaction decreases the amount of free sialic acid released through the neuraminidase reaction. We conclude that a single enzyme can catalyze the transfer or the hydrolysis of macromolecular-bound sialic acid. The predominant direction of the reaction will depend on the availability of appropriate oligosaccharide acceptors of sialic acid.
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spelling pubmed-21191312008-04-16 Trypanosoma cruzi trans-sialidase and neuraminidase activities can be mediated by the same enzymes J Exp Med Articles Trans-sialidase and neuraminidase activities have been detected on the surface membrane of trypomastigotes of Trypanosoma cruzi, and both have been implicated in the parasite's invasion of host cells. We show here that these enzymes are structurally related. They are recognized by two independently derived monoclonal antibodies, are anchored to the membrane by glycosylphosphatidylinositol, copurify by ion exchange, molecular sieving, and hydrophobic chromatography, have maximal activities between pH 6.5 and 7.5, and are inactivated by heating at 56 degrees C. Furthermore, the neuraminidase and trans-sialidase reactions are coupled. An increase of the concentration of acceptors of the transfer reaction decreases the amount of free sialic acid released through the neuraminidase reaction. We conclude that a single enzyme can catalyze the transfer or the hydrolysis of macromolecular-bound sialic acid. The predominant direction of the reaction will depend on the availability of appropriate oligosaccharide acceptors of sialic acid. The Rockefeller University Press 1992-02-01 /pmc/articles/PMC2119131/ /pubmed/1732417 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Trypanosoma cruzi trans-sialidase and neuraminidase activities can be mediated by the same enzymes
title Trypanosoma cruzi trans-sialidase and neuraminidase activities can be mediated by the same enzymes
title_full Trypanosoma cruzi trans-sialidase and neuraminidase activities can be mediated by the same enzymes
title_fullStr Trypanosoma cruzi trans-sialidase and neuraminidase activities can be mediated by the same enzymes
title_full_unstemmed Trypanosoma cruzi trans-sialidase and neuraminidase activities can be mediated by the same enzymes
title_short Trypanosoma cruzi trans-sialidase and neuraminidase activities can be mediated by the same enzymes
title_sort trypanosoma cruzi trans-sialidase and neuraminidase activities can be mediated by the same enzymes
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2119131/
https://www.ncbi.nlm.nih.gov/pubmed/1732417