Please use this identifier to cite or link to this item: https://www.arca.fiocruz.br/handle/icict/19553
Title: A Proteolytic Fragment of Trypanosoma cruzi trans-Sialidase Lacking the Carboxyl-terminal Domain Is Active, Monomeric, and Generates Antibodies That Inhibit Enzymatic Activity
Authors: Schenkman, Sergio
Chaves, Luciana Botelho
Pontes-de-Carvalho, Lain Carlos
Eichinged, Daniel
Affilliation: Escola Paulista de Medicina. Department of Microbiology, Immunology and Parasitology. São Paulo, SP, Brazil
Escola Paulista de Medicina. Department of Microbiology, Immunology and Parasitology. São Paulo, SP, Brazil
New York University Medical Center. Michael Heidelberger Division of Immunology. New York, New York
New York University Medical Center. Michael Heidelberger Division of Immunology. New York, New York
Abstract: trans-Sialidase isolated from trypomastigote forms of IlZypanosoma cruzi, the protozoan parasite that causes Chagas’ disease, is multimeric and heterogeneous in size. We show here that limited proteolysis of trans-sialidase with papain yields a single monomeric polypeptide chain of 70 kDa that conserves full enzymatic activity on soluble and membrane-bound substrates. The papain fragment lacks most otfh e 12-amino acid repeats of the carboxyl-terminal domain that comprises about 50% of the native trans-sialidase. When injected into rabbits, the papain-generated fragmenitn duces antibodies that inhibit trans-sialidase activity and trypomastigote sialylation. The repeats are also not required for the stability of the enzyme or fotrh e correct folding during the biosynthesis in Escherichia coli, but seem essential for trans-sialidase oligomerization. We conclude that transsialidase is composed of two structurally and functionally independent domains.
Keywords: Trypanosoma cruzi
Chagas disease
Sialidase
Enzyme
Sialic acid
keywords: Trypanosoma cruzi
Doença de Chagas
Sialidase
Enzima
Ácido siálico
Issue Date: 1994
Publisher: American Society for Biochemistry and Molecular Biology
Citation: SCHENKMAN, S. et al. A Proteolytic fragment of Trypanosoma cruzi trans-sialidase lacking the carboxyl-terminal domain is active, monomeric, and generates antibodies that inhibit enzymatic activity. Journal of Biological Chemistry, v. 269, n. 11, p. 7970-7975, 1994.
Description: Pontes-de-Carvalho, Lain Carlos “Documento produzido em parceria ou por autor vinculado à Fiocruz, mas não consta à informação no documento”.
ISSN: 0021-9258
Copyright: open access
Appears in Collections:BA - IGM - Artigos de Periódicos

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