A Proteolytic Fragment of Trypanosoma cruzi trans-Sialidase Lacking the Carboxyl-terminal Domain Is Active, Monomeric, and Generates Antibodies That Inhibit Enzymatic Activity
Autor(a) principal: | |
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Data de Publicação: | 1994 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da FIOCRUZ (ARCA) |
Texto Completo: | https://www.arca.fiocruz.br/handle/icict/19553 |
Resumo: | Pontes-de-Carvalho, Lain Carlos “Documento produzido em parceria ou por autor vinculado à Fiocruz, mas não consta à informação no documento”. |
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Schenkman, SergioChaves, Luciana BotelhoPontes-de-Carvalho, Lain CarlosEichinged, Daniel2017-06-28T14:30:44Z2017-06-28T14:30:44Z1994SCHENKMAN, 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, 1994.0021-9258https://www.arca.fiocruz.br/handle/icict/19553Pontes-de-Carvalho, Lain Carlos “Documento produzido em parceria ou por autor vinculado à Fiocruz, mas não consta à informação no documento”.Fundação de Amparo a Pesquisa do Estado de São Paulo, Conselho Nacional de Desenvolvimento Cientifico e Tecnológico, UNDPMorld BanWWHO Special Program for Research and Training in Tropical Diseases, TheRockefeller Foundation.Escola Paulista de Medicina. Department of Microbiology, Immunology and Parasitology. São Paulo, SP, BrazilEscola Paulista de Medicina. Department of Microbiology, Immunology and Parasitology. São Paulo, SP, BrazilNew York University Medical Center. Michael Heidelberger Division of Immunology. New York, New YorkNew York University Medical Center. Michael Heidelberger Division of Immunology. New York, New Yorktrans-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.engAmerican Society for Biochemistry and Molecular BiologyTrypanosoma cruziDoença de ChagasSialidaseEnzimaÁcido siálicoTrypanosoma cruziChagas diseaseSialidaseEnzymeSialic acidA Proteolytic Fragment of Trypanosoma cruzi trans-Sialidase Lacking the Carboxyl-terminal Domain Is Active, Monomeric, and Generates Antibodies That Inhibit Enzymatic Activityinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da FIOCRUZ (ARCA)instname:Fundação Oswaldo Cruz (FIOCRUZ)instacron:FIOCRUZLICENSElicense.txtlicense.txttext/plain; charset=utf-82991https://www.arca.fiocruz.br/bitstream/icict/19553/1/license.txt5a560609d32a3863062d77ff32785d58MD51ORIGINALSchenkman S A proteolytic fragment of the... .pdfSchenkman S A proteolytic fragment of the... 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dc.title.pt_BR.fl_str_mv |
A Proteolytic Fragment of Trypanosoma cruzi trans-Sialidase Lacking the Carboxyl-terminal Domain Is Active, Monomeric, and Generates Antibodies That Inhibit Enzymatic Activity |
title |
A Proteolytic Fragment of Trypanosoma cruzi trans-Sialidase Lacking the Carboxyl-terminal Domain Is Active, Monomeric, and Generates Antibodies That Inhibit Enzymatic Activity |
spellingShingle |
A Proteolytic Fragment of Trypanosoma cruzi trans-Sialidase Lacking the Carboxyl-terminal Domain Is Active, Monomeric, and Generates Antibodies That Inhibit Enzymatic Activity Schenkman, Sergio Trypanosoma cruzi Doença de Chagas Sialidase Enzima Ácido siálico Trypanosoma cruzi Chagas disease Sialidase Enzyme Sialic acid |
title_short |
A Proteolytic Fragment of Trypanosoma cruzi trans-Sialidase Lacking the Carboxyl-terminal Domain Is Active, Monomeric, and Generates Antibodies That Inhibit Enzymatic Activity |
title_full |
A Proteolytic Fragment of Trypanosoma cruzi trans-Sialidase Lacking the Carboxyl-terminal Domain Is Active, Monomeric, and Generates Antibodies That Inhibit Enzymatic Activity |
title_fullStr |
A Proteolytic Fragment of Trypanosoma cruzi trans-Sialidase Lacking the Carboxyl-terminal Domain Is Active, Monomeric, and Generates Antibodies That Inhibit Enzymatic Activity |
title_full_unstemmed |
A Proteolytic Fragment of Trypanosoma cruzi trans-Sialidase Lacking the Carboxyl-terminal Domain Is Active, Monomeric, and Generates Antibodies That Inhibit Enzymatic Activity |
title_sort |
A Proteolytic Fragment of Trypanosoma cruzi trans-Sialidase Lacking the Carboxyl-terminal Domain Is Active, Monomeric, and Generates Antibodies That Inhibit Enzymatic Activity |
author |
Schenkman, Sergio |
author_facet |
Schenkman, Sergio Chaves, Luciana Botelho Pontes-de-Carvalho, Lain Carlos Eichinged, Daniel |
author_role |
author |
author2 |
Chaves, Luciana Botelho Pontes-de-Carvalho, Lain Carlos Eichinged, Daniel |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Schenkman, Sergio Chaves, Luciana Botelho Pontes-de-Carvalho, Lain Carlos Eichinged, Daniel |
dc.subject.other.pt_BR.fl_str_mv |
Trypanosoma cruzi Doença de Chagas Sialidase Enzima Ácido siálico |
topic |
Trypanosoma cruzi Doença de Chagas Sialidase Enzima Ácido siálico Trypanosoma cruzi Chagas disease Sialidase Enzyme Sialic acid |
dc.subject.en.pt_BR.fl_str_mv |
Trypanosoma cruzi Chagas disease Sialidase Enzyme Sialic acid |
description |
Pontes-de-Carvalho, Lain Carlos “Documento produzido em parceria ou por autor vinculado à Fiocruz, mas não consta à informação no documento”. |
publishDate |
1994 |
dc.date.issued.fl_str_mv |
1994 |
dc.date.accessioned.fl_str_mv |
2017-06-28T14:30:44Z |
dc.date.available.fl_str_mv |
2017-06-28T14:30:44Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
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. |
dc.identifier.uri.fl_str_mv |
https://www.arca.fiocruz.br/handle/icict/19553 |
dc.identifier.issn.pt_BR.fl_str_mv |
0021-9258 |
identifier_str_mv |
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. 0021-9258 |
url |
https://www.arca.fiocruz.br/handle/icict/19553 |
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eng |
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eng |
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info:eu-repo/semantics/openAccess |
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openAccess |
dc.publisher.none.fl_str_mv |
American Society for Biochemistry and Molecular Biology |
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American Society for Biochemistry and Molecular Biology |
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