Receptor-binding variants of H3N2 influenza A viruses: characterization of their sialidase activity towards different substrates

Detalhes bibliográficos
Autor(a) principal: Couto, Alessanda Abdo do
Data de Publicação: 2004
Outros Autores: Barros, José Júnior França de, Couceiro, José Nelson dos Santos Silva
Tipo de documento: Artigo
Idioma: por
Título da fonte: Repositório Institucional da UFBA
Texto Completo: http://repositorio.ufba.br/ri/handle/ri/20341
Resumo: Artigo original (p.13-19)
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spelling Couto, Alessanda Abdo doBarros, José Júnior França deCouceiro, José Nelson dos Santos SilvaCouto, Alessanda Abdo doBarros, José Júnior França deCouceiro, José Nelson dos Santos Silva2016-09-13T15:08:36Z2016-09-13T15:08:36Z2004COUTO, A. A. do. Receptor-binding variants of H3N2 influenza A viruses: characterization of their sialidase activity towards different substrates. R. Ci. méd. biol., Salvador, v. 3, n. 1, p. 13-19, jan./jun. 2004.2236-5222http://repositorio.ufba.br/ri/handle/ri/20341v.3, n.1Artigo original (p.13-19)Influenza virus sialidase develops an essential activity on cellular glycoproteins, then permitting the dissemination of the virus infections by preventing virus-virus self aggregation and virus-cell rebinding. Two purified variant samples of influenza A/Memphis/102/72 (H3N2) viruses, which are recognized for their receptor-binding activity to a-2,6 or a- 2,3-sialyllactose structures, were analysed for their sialidase activity on different natural and artificial substrates. The M1/ 5 sample exhibited higher sialidase activity on fetuin (O.D.=0.226), MPN (O.D.=0.110) and human erythrocytes (10,240 HAU/ml), while the activity of the M1/5HS8 sample on these substrates was expressed by O.D.=0.129, O.D.=0.065 and 2,560 HAU/ml when using fetuin, MPN and human erythrocytes as substrates, respectively. However, the M1/5HS8 sample showed more significative sialidase activity on mucin when compared to the M1/5 sample: the enzyme activity of first sample was responsible for liberation of 3.5 nmol of free sialic acids while the last one produced 16.5 nmol of free sialic acidsSubmitted by ROBERTO PAULO CORREIA DE ARAÚJO (ppgorgsistem@ufba.br) on 2016-09-13T15:08:36Z No. of bitstreams: 1 R. Ci. méd. biol., v.3, n. 1-2004.pdf: 68489 bytes, checksum: ec482474a61fcf3e7bff2d7bf75ee293 (MD5)Made available in DSpace on 2016-09-13T15:08:36Z (GMT). No. of bitstreams: 1 R. Ci. méd. biol., v.3, n. 1-2004.pdf: 68489 bytes, checksum: ec482474a61fcf3e7bff2d7bf75ee293 (MD5) Previous issue date: 2004-01SalvadorInstituto de Ciências da Saúde/ Universidade Federal da Bahiahttp://www.portalseer.ufba.br/index.php/cmbio/issue/view/498/showTocreponame:Repositório Institucional da UFBAinstname:Universidade Federal da Bahia (UFBA)instacron:UFBAInfluenza virus.Receptor-binding variants.Neuraminidase (NA).Natural and artificial substrates.Receptor-binding variants of H3N2 influenza A viruses: characterization of their sialidase activity towards different substratesRevista de Ciências Médicas e Biológicasinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleinfo:eu-repo/semantics/openAccessporORIGINALR. Ci. méd. biol., v.3, n. 1-2004.pdfR. 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dc.title.pt_BR.fl_str_mv Receptor-binding variants of H3N2 influenza A viruses: characterization of their sialidase activity towards different substrates
dc.title.alternative.pt_BR.fl_str_mv Revista de Ciências Médicas e Biológicas
title Receptor-binding variants of H3N2 influenza A viruses: characterization of their sialidase activity towards different substrates
spellingShingle Receptor-binding variants of H3N2 influenza A viruses: characterization of their sialidase activity towards different substrates
Couto, Alessanda Abdo do
Influenza virus.
Receptor-binding variants.
Neuraminidase (NA).
Natural and artificial substrates.
title_short Receptor-binding variants of H3N2 influenza A viruses: characterization of their sialidase activity towards different substrates
title_full Receptor-binding variants of H3N2 influenza A viruses: characterization of their sialidase activity towards different substrates
title_fullStr Receptor-binding variants of H3N2 influenza A viruses: characterization of their sialidase activity towards different substrates
title_full_unstemmed Receptor-binding variants of H3N2 influenza A viruses: characterization of their sialidase activity towards different substrates
title_sort Receptor-binding variants of H3N2 influenza A viruses: characterization of their sialidase activity towards different substrates
author Couto, Alessanda Abdo do
author_facet Couto, Alessanda Abdo do
Barros, José Júnior França de
Couceiro, José Nelson dos Santos Silva
author_role author
author2 Barros, José Júnior França de
Couceiro, José Nelson dos Santos Silva
author2_role author
author
dc.contributor.author.fl_str_mv Couto, Alessanda Abdo do
Barros, José Júnior França de
Couceiro, José Nelson dos Santos Silva
Couto, Alessanda Abdo do
Barros, José Júnior França de
Couceiro, José Nelson dos Santos Silva
dc.subject.por.fl_str_mv Influenza virus.
Receptor-binding variants.
Neuraminidase (NA).
Natural and artificial substrates.
topic Influenza virus.
Receptor-binding variants.
Neuraminidase (NA).
Natural and artificial substrates.
description Artigo original (p.13-19)
publishDate 2004
dc.date.issued.fl_str_mv 2004
dc.date.accessioned.fl_str_mv 2016-09-13T15:08:36Z
dc.date.available.fl_str_mv 2016-09-13T15:08:36Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
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dc.identifier.citation.fl_str_mv COUTO, A. A. do. Receptor-binding variants of H3N2 influenza A viruses: characterization of their sialidase activity towards different substrates. R. Ci. méd. biol., Salvador, v. 3, n. 1, p. 13-19, jan./jun. 2004.
dc.identifier.uri.fl_str_mv http://repositorio.ufba.br/ri/handle/ri/20341
dc.identifier.issn.none.fl_str_mv 2236-5222
dc.identifier.number.pt_BR.fl_str_mv v.3, n.1
identifier_str_mv COUTO, A. A. do. Receptor-binding variants of H3N2 influenza A viruses: characterization of their sialidase activity towards different substrates. R. Ci. méd. biol., Salvador, v. 3, n. 1, p. 13-19, jan./jun. 2004.
2236-5222
v.3, n.1
url http://repositorio.ufba.br/ri/handle/ri/20341
dc.language.iso.fl_str_mv por
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dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
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dc.publisher.none.fl_str_mv Instituto de Ciências da Saúde/ Universidade Federal da Bahia
publisher.none.fl_str_mv Instituto de Ciências da Saúde/ Universidade Federal da Bahia
dc.source.pt_BR.fl_str_mv http://www.portalseer.ufba.br/index.php/cmbio/issue/view/498/showToc
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