A Proteolytic Fragment of Trypanosoma cruzi trans-Sialidase Lacking the Carboxyl-terminal Domain Is Active, Monomeric, and Generates Antibodies That Inhibit Enzymatic Activity

Detalhes bibliográficos
Autor(a) principal: Schenkman, Sergio
Data de Publicação: 1994
Outros Autores: Chaves, Luciana Botelho, Pontes-de-Carvalho, Lain Carlos, Eichinged, Daniel
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”.
id CRUZ_5cafe5a49510de97d46eb21cab1b4d4b
oai_identifier_str oai:www.arca.fiocruz.br:icict/19553
network_acronym_str CRUZ
network_name_str Repositório Institucional da FIOCRUZ (ARCA)
repository_id_str 2135
spelling 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... .pdfapplication/pdf5141621https://www.arca.fiocruz.br/bitstream/icict/19553/2/Schenkman%20S%20A%20proteolytic%20fragment%20of%20the...%20.pdf0cbbc540f49ef4a7b9adf718410ff688MD52TEXTSchenkman S A proteolytic fragment of the... .pdf.txtSchenkman S A proteolytic fragment of the... .pdf.txtExtracted texttext/plain43583https://www.arca.fiocruz.br/bitstream/icict/19553/3/Schenkman%20S%20A%20proteolytic%20fragment%20of%20the...%20.pdf.txt904b1efa41bda655d4941e9b70859a82MD53icict/195532023-03-15 14:33:29.998oai:www.arca.fiocruz.br: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ório InstitucionalPUBhttps://www.arca.fiocruz.br/oai/requestrepositorio.arca@fiocruz.bropendoar:21352023-03-15T17:33:29Repositório Institucional da FIOCRUZ (ARCA) - Fundação Oswaldo Cruz (FIOCRUZ)false
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
dc.language.iso.fl_str_mv eng
language eng
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
dc.source.none.fl_str_mv reponame:Repositório Institucional da FIOCRUZ (ARCA)
instname:Fundação Oswaldo Cruz (FIOCRUZ)
instacron:FIOCRUZ
instname_str Fundação Oswaldo Cruz (FIOCRUZ)
instacron_str FIOCRUZ
institution FIOCRUZ
reponame_str Repositório Institucional da FIOCRUZ (ARCA)
collection Repositório Institucional da FIOCRUZ (ARCA)
bitstream.url.fl_str_mv https://www.arca.fiocruz.br/bitstream/icict/19553/1/license.txt
https://www.arca.fiocruz.br/bitstream/icict/19553/2/Schenkman%20S%20A%20proteolytic%20fragment%20of%20the...%20.pdf
https://www.arca.fiocruz.br/bitstream/icict/19553/3/Schenkman%20S%20A%20proteolytic%20fragment%20of%20the...%20.pdf.txt
bitstream.checksum.fl_str_mv 5a560609d32a3863062d77ff32785d58
0cbbc540f49ef4a7b9adf718410ff688
904b1efa41bda655d4941e9b70859a82
bitstream.checksumAlgorithm.fl_str_mv MD5
MD5
MD5
repository.name.fl_str_mv Repositório Institucional da FIOCRUZ (ARCA) - Fundação Oswaldo Cruz (FIOCRUZ)
repository.mail.fl_str_mv repositorio.arca@fiocruz.br
_version_ 1798324996995547136