Publicação
Trypanosoma cruzi Trans-sialidase and Neuraminidase Activities Can Be Mediated by the Same Enzymes
| Resumo: | Pontes-de-Carvalho, L. C. “Documento produzido em parceria ou por autor vinculado à Fiocruz, mas não consta à informação no documento”. |
|---|---|
| Autores principais: | Schenkman, Sergio |
| Outros Autores: | Pontes-de-Carvalho, Lain Carlos; Nussenzweig, Victor |
| Assunto: | Trypanosoma cruzi Enzimas Ácido siálico Hidrólise Trypanosoma cruzi Enzymes Sialic acid Hydrolysis |
| Ano: | 2017 |
| País: | Brasil |
| Tipo de documento: | artigo |
| Tipo de acesso: | acesso aberto |
| Instituição associada: | IBICT |
| Idioma: | inglês |
| Origem: | Oasisbr |
| _version_ | 1871529629162930176 |
|---|---|
| author | Schenkman, Sergio |
| author2 | Pontes-de-Carvalho, Lain Carlos Nussenzweig, Victor |
| author2_role | author author |
| author_facet | Schenkman, Sergio Pontes-de-Carvalho, Lain Carlos Nussenzweig, Victor |
| author_role | author |
| country_str | BR |
| creators_json_txt | [{\"Person.name\":\"Schenkman, Sergio\"},{\"Person.name\":\"Pontes-de-Carvalho, Lain Carlos\"},{\"Person.name\":\"Nussenzweig, Victor\"}] |
| datacite.creators.creator.creatorName.fl_str_mv | Schenkman, Sergio Pontes-de-Carvalho, Lain Carlos Nussenzweig, Victor |
| datacite.date.Accepted.fl_str_mv | 1992-01-01T00:00:00Z |
| datacite.date.available.fl_str_mv | 2017-06-21T18:15:24Z |
| datacite.date.embargoed.fl_str_mv | 2017-06-21T18:15:24Z |
| datacite.rights.fl_str_mv | http://purl.org/coar/access_right/c_abf2 |
| datacite.subjects.subject.fl_str_mv | Trypanosoma cruzi Enzimas Ácido siálico Hidrólise Trypanosoma cruzi Enzymes Sialic acid Hydrolysis |
| datacite.titles.title.fl_str_mv | Trypanosoma cruzi Trans-sialidase and Neuraminidase Activities Can Be Mediated by the Same Enzymes |
| dc.creator.none.fl_str_mv | Schenkman, Sergio Pontes-de-Carvalho, Lain Carlos Nussenzweig, Victor |
| dc.date.Accepted.fl_str_mv | 1992-01-01T00:00:00Z |
| dc.date.available.fl_str_mv | 2017-06-21T18:15:24Z |
| dc.date.embargoed.fl_str_mv | 2017-06-21T18:15:24Z |
| dc.description.none.fl_str_mv | MacArthur Foundation, the UNDP/World Bank/WHO Special Program for Research and Training in Tropical Diseases, Conselho Nacional de Desenvolvimento Científico e Tecnologico, Secretaria de Ciencia e Tecnologia (programa RHAE), and Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (Brazil). Escola Paulista de Medicina. São Paulo, SP, 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 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~ Furthermore, the neuraminidase and trans-sialidase reactions are coupled. An increase of the concentration of acceptors of the transfer reaction decreases the amount of flee 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. |
| dc.identifier.none.fl_str_mv | https://www.arca.fiocruz.br/handle/icict/19476 |
| dc.language.none.fl_str_mv | eng |
| dc.publisher.none.fl_str_mv | Rockefeller University Press |
| dc.rights.none.fl_str_mv | http://purl.org/coar/access_right/c_abf2 |
| dc.source.none.fl_str_mv | reponame:Repositório Institucional da FIOCRUZ (ARCA) instname:Fundação Oswaldo Cruz (FIOCRUZ) instacron:FIOCRUZ |
| dc.subject.none.fl_str_mv | Trypanosoma cruzi Enzimas Ácido siálico Hidrólise Trypanosoma cruzi Enzymes Sialic acid Hydrolysis |
| dc.title.fl_str_mv | Trypanosoma cruzi Trans-sialidase and Neuraminidase Activities Can Be Mediated by the Same Enzymes |
| dc.type.none.fl_str_mv | http://purl.org/coar/resource_type/c_6501 |
| description | Pontes-de-Carvalho, L. C. “Documento produzido em parceria ou por autor vinculado à Fiocruz, mas não consta à informação no documento”. |
| dirty | 0 |
| eu_rights_str_mv | openAccess |
| format | article |
| id | oasisbr_c8ef560787f3e673f2eef3b41cd8a441 |
| identifier.url.fl_str_mv | https://www.arca.fiocruz.br/handle/icict/19476 |
| inst_facet_str | urn:organizationAcronym:oasisbr{{{_:::_}}}IBICT |
| instacron_str | OASISBR |
| institution | IBICT |
| instname_str | IBICT |
| language | eng |
| network_acronym_str | oasisbr |
| network_name_str | Oasisbr |
| oai_identifier_str | oai:www.arca.fiocruz.br:icict/19476 |
| organization_str_mv | urn:organizationAcronym:oasisbr |
| person_str_mv | Schenkman, Sergio Pontes-de-Carvalho, Lain Carlos Nussenzweig, Victor |
| publishDate | 2017 |
| publisher.none.fl_str_mv | Rockefeller University Press |
| repo_facet_str | urn:repositoryAcronym:oasisbr{{{_:::_}}}Oasisbr |
| reponame_str | Oasisbr |
| repository_id_str | urn:repositoryAcronym:oasisbr |
| service_str_mv | urn:repositoryAcronym:oasisbr |
| spelling | Trypanosoma cruzi Trans-sialidase and Neuraminidase Activities Can Be Mediated by the Same EnzymesSchenkman, SergioPontes-de-Carvalho, Lain CarlosNussenzweig, VictorTrypanosoma cruziEnzimasÁcido siálicoHidróliseTrypanosoma cruziEnzymesSialic acidHydrolysisopen accesshttp://purl.org/coar/access_right/c_abf2https://www.arca.fiocruz.br/handle/icict/19476URLSCHENKMAN, S.; PONTES-DE-CARVALHO, L. C.; NUSSENZWEIG, V. Trypanosoma cruzi Trans-sialidase and Neuraminidase Activities Can Be Mediated by the Same Enzymes. Journal of Experimental Medicine, v. 175, p. 567-575, 1992.N/AHasVersionhttps://www.arca.fiocruz.br/handle/icict/19476URLHasVersion0022-1007N/AHasVersion2017-06-21T18:15:24Z2017-06-211992-01-01T00:00:00ZPontes-de-Carvalho, L. C. “Documento produzido em parceria ou por autor vinculado à Fiocruz, mas não consta à informação no documento”.MacArthur Foundation, the UNDP/World Bank/WHO Special Program for Research and Training in Tropical Diseases, Conselho Nacional de Desenvolvimento Científico e Tecnologico, Secretaria de Ciencia e Tecnologia (programa RHAE), and Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (Brazil).Escola Paulista de Medicina. São Paulo, SP, BrasilNew York University Medical Center. Department of Pathology and Kaplan Cancer Center. New York, New YorkNew York University Medical Center. Department of Pathology and Kaplan Cancer Center. New York, New YorkTrans-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~ Furthermore, the neuraminidase and trans-sialidase reactions are coupled. An increase of the concentration of acceptors of the transfer reaction decreases the amount of flee 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.engRockefeller University Pressreponame:Repositório Institucional da FIOCRUZ (ARCA)instname:Fundação Oswaldo Cruz (FIOCRUZ)instacron:FIOCRUZVoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85journal articlehttp://purl.org/coar/resource_type/c_6501literature |
| spellingShingle | Trypanosoma cruzi Trans-sialidase and Neuraminidase Activities Can Be Mediated by the Same Enzymes Schenkman, Sergio Trypanosoma cruzi Enzimas Ácido siálico Hidrólise Trypanosoma cruzi Enzymes Sialic acid Hydrolysis |
| status | SINGLETON |
| status_str | VoR |
| subject.fl_str_mv | Trypanosoma cruzi Enzimas Ácido siálico Hidrólise Trypanosoma cruzi Enzymes Sialic acid Hydrolysis |
| 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 | Trypanosoma cruzi Enzimas Ácido siálico Hidrólise Trypanosoma cruzi Enzymes Sialic acid Hydrolysis |
| topic_facet | Trypanosoma cruzi Enzimas Ácido siálico Hidrólise Trypanosoma cruzi Enzymes Sialic acid Hydrolysis |
| url | https://www.arca.fiocruz.br/handle/icict/19476 |
| visible | 1 |
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