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https://www.arca.fiocruz.br/handle/icict/8338
CHARACTERIZATION OF A NOVEL TRANS-SIALIDASE OF TRYPANOSOMA BRUCEI PROCYCLIC TRYPOMASTIGOTES AND IDENTIFICATION OF PROCYCLIN AS THE MAIN SIALIC ACID ACCEPTOR.
Sialiltransferases/metabolismo
Trypanosoma brucei brucei/enzimologia
Glicoproteínas Variantes de Superfície de Trypanosoma/metabolismo
Animais
Neuraminidase/metabolismo
Proteínas de Protozoários/isolamento & purificação
Proteínas de Protozoários/metabolismo
Ácidos Siálicos/metabolismo
Sialoglicoproteínas/metabolismo
Sialiltransferases/isolamento & purificação
Trypanosoma brucei brucei/citologia
Trypanosoma cruzi/enzimologia
Autor(es)
Afiliação
New York University Medical Center. Department of Pathology and Kaplan Cancer Center. New York, New York / Fundação Oswaldo Cruz. Centro de Pesquisa Gonçalo Moniz. Salvador, BA, Brasil
New York University Medical Center. Department of Pathology and Kaplan Cancer Center. New York, New York
New York University Medical Center. Department of Pathology and Kaplan Cancer Center. New York, New York
New York University Medical Center. Department of Medical and Molecular Parasitology. New York, New York
New York University Medical Center. Department of Medical and Molecular Parasitology. New York, New York
The Johns Hopkins University. Department of Biological Chemistry. Baltimore, Maryland
The Johns Hopkins University. Baltimore, Maryland
New York University Medical Center. Department of Pathology and Kaplan Cancer Center. New York, New York
New York University Medical Center. Department of Pathology and Kaplan Cancer Center. New York, New York
New York University Medical Center. Department of Pathology and Kaplan Cancer Center. New York, New York
New York University Medical Center. Department of Medical and Molecular Parasitology. New York, New York
New York University Medical Center. Department of Medical and Molecular Parasitology. New York, New York
The Johns Hopkins University. Department of Biological Chemistry. Baltimore, Maryland
The Johns Hopkins University. Baltimore, Maryland
New York University Medical Center. Department of Pathology and Kaplan Cancer Center. New York, New York
Resumo em Inglês
Here we report the presence of a trans-sialidase on the surface of Trypanosoma brucei culturederived
procyclic trypomastigotes. The enzyme is not detected in lysates of bloodstream trypomastigotes
enriched for either stumpy or slender forms. The trans-sialidase catalyzes the transfer
of ot(2-3)-linked sialic acid residues to lactose./3-galactopyranosyl residues are at least 100 times
better acceptors for sialic acid than ot-galactopyranosyl residues. In the absence of efficient acceptors,
the purified enzyme transfers sialic acid to water, i.e., it acts as a sialidase. Although the T. cruzi
and T. brucei trans-sialidases have very similar donor and acceptor specificities, they are antigenicaUy
distinct. Sodium dodecyl sulfate--polyacramide gel electrophoresis under nonreducing conditions
and silver staining of the purified trans-sialidase reveals a single band of 63 kD. When the surface
membrane of live procyclic trypomastigotes is trans-sialylated, using radioactive sialyllactose as
the donor substrate, it appears that the only sialylated surface molecule is procyclin. Pronase
treatment of live parasites removes only part of the surface sialic acid, in agreement with recent
data showing that the glycosylphosphatidylinositol anchor of procyclin is sialylated (Ferguson, M. A. J., M. Murray, H. Rutherford, and M. J. McConville. 1993. Biochem. J. In press).
DeCS
Glicoproteínas de MembranaSialiltransferases/metabolismo
Trypanosoma brucei brucei/enzimologia
Glicoproteínas Variantes de Superfície de Trypanosoma/metabolismo
Animais
Neuraminidase/metabolismo
Proteínas de Protozoários/isolamento & purificação
Proteínas de Protozoários/metabolismo
Ácidos Siálicos/metabolismo
Sialoglicoproteínas/metabolismo
Sialiltransferases/isolamento & purificação
Trypanosoma brucei brucei/citologia
Trypanosoma cruzi/enzimologia
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