Lepstospira interrogans shotgun phage display identified LigB as a heparin-binding protein
Autor(a) principal: | |
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Data de Publicação: | 2012 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | http://repositorio.unifesp.br/handle/11600/35497 http://dx.doi.org/10.1016/j.bbrc.2012.09.137 |
Resumo: | LigB is an adhesin from pathogenic Leptospira that is able to bind to extracellular matrix and is considered a virulence factor. A shotgun phage display genomic library was constructed and used for panning against Heparan Sulfate Proteoglycan (HSPG). A phage clone encoding part of LigB protein was selected in panning experiments and showed specific binding to heparin. To validate the selected clone, fragments of LigB were produced as recombinant proteins and showed affinity to heparin and to mammalian cells. Heparin was also able to reduce the binding of rLB-Ct to mammalian cells. Our data suggests that the glycosaminoglycan moiety of the HSPG is responsible for its binding and could mediate the attachment of the recombinant protein rLB-Ct. Thus, heparin may act as a receptor for Leptospira to colonize and to invade the host tissue. (C) 2012 Elsevier Inc. All rights reserved. |
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Ching Ching, Ana TungFavaro, Regiane DeganLima, Swiany SilveiraMuniz Chaves, Agtha de AlencarLima, Marcelo Andrade de [UNIFESP]Nader, Helena Bonciani [UNIFESP]Estima Abreu, Patricia A.Ho, Paulo LeeInst ButantanUniversidade de São Paulo (USP)Universidade Federal de São Paulo (UNIFESP)2016-01-24T14:27:59Z2016-01-24T14:27:59Z2012-11-02Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 427, n. 4, p. 774-779, 2012.0006-291Xhttp://repositorio.unifesp.br/handle/11600/35497http://dx.doi.org/10.1016/j.bbrc.2012.09.137WOS000311134700016.pdf10.1016/j.bbrc.2012.09.137WOS:000311134700016LigB is an adhesin from pathogenic Leptospira that is able to bind to extracellular matrix and is considered a virulence factor. A shotgun phage display genomic library was constructed and used for panning against Heparan Sulfate Proteoglycan (HSPG). A phage clone encoding part of LigB protein was selected in panning experiments and showed specific binding to heparin. To validate the selected clone, fragments of LigB were produced as recombinant proteins and showed affinity to heparin and to mammalian cells. Heparin was also able to reduce the binding of rLB-Ct to mammalian cells. Our data suggests that the glycosaminoglycan moiety of the HSPG is responsible for its binding and could mediate the attachment of the recombinant protein rLB-Ct. Thus, heparin may act as a receptor for Leptospira to colonize and to invade the host tissue. (C) 2012 Elsevier Inc. All rights reserved.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Fundacao ButantanInst Butantan, Ctr Biotecnol, BR-05503900 São Paulo, BrazilUniv São Paulo, Programa Posgrad Interunidades Biotecnol, IPT, Inst Butantan,Inst Ciencias Biomed, BR-05508900 São Paulo, BrazilUniv São Paulo, Inst Quim, Dept Bioquim, BR-05508000 São Paulo, BrazilUniversidade Federal de São Paulo, Dept Bioquim, Disciplina Biol Mol, BR-04044020 São Paulo, BrazilInst Butantan, Lab Bacteriol, BR-05503900 São Paulo, BrazilUniversidade Federal de São Paulo, Dept Bioquim, Disciplina Biol Mol, BR-04044020 São Paulo, BrazilWeb of Science774-779engElsevier B.V.Biochemical and Biophysical Research Communicationshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policyinfo:eu-repo/semantics/openAccessLeptospira interrogansHeparinPhage displayLigBLepstospira interrogans shotgun phage display identified LigB as a heparin-binding proteininfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlereponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESPORIGINALWOS000311134700016.pdfapplication/pdf489724${dspace.ui.url}/bitstream/11600/35497/1/WOS000311134700016.pdf2918bd1f1a57bf2111c351b6381f22beMD51open accessTEXTWOS000311134700016.pdf.txtWOS000311134700016.pdf.txtExtracted texttext/plain32151${dspace.ui.url}/bitstream/11600/35497/2/WOS000311134700016.pdf.txt40cca642bd5698b8dcaf0b7345189f60MD52open access11600/354972022-09-27 10:14:38.747open accessoai:repositorio.unifesp.br:11600/35497Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652022-09-27T13:14:38Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.en.fl_str_mv |
Lepstospira interrogans shotgun phage display identified LigB as a heparin-binding protein |
title |
Lepstospira interrogans shotgun phage display identified LigB as a heparin-binding protein |
spellingShingle |
Lepstospira interrogans shotgun phage display identified LigB as a heparin-binding protein Ching Ching, Ana Tung Leptospira interrogans Heparin Phage display LigB |
title_short |
Lepstospira interrogans shotgun phage display identified LigB as a heparin-binding protein |
title_full |
Lepstospira interrogans shotgun phage display identified LigB as a heparin-binding protein |
title_fullStr |
Lepstospira interrogans shotgun phage display identified LigB as a heparin-binding protein |
title_full_unstemmed |
Lepstospira interrogans shotgun phage display identified LigB as a heparin-binding protein |
title_sort |
Lepstospira interrogans shotgun phage display identified LigB as a heparin-binding protein |
author |
Ching Ching, Ana Tung |
author_facet |
Ching Ching, Ana Tung Favaro, Regiane Degan Lima, Swiany Silveira Muniz Chaves, Agtha de Alencar Lima, Marcelo Andrade de [UNIFESP] Nader, Helena Bonciani [UNIFESP] Estima Abreu, Patricia A. Ho, Paulo Lee |
author_role |
author |
author2 |
Favaro, Regiane Degan Lima, Swiany Silveira Muniz Chaves, Agtha de Alencar Lima, Marcelo Andrade de [UNIFESP] Nader, Helena Bonciani [UNIFESP] Estima Abreu, Patricia A. Ho, Paulo Lee |
author2_role |
author author author author author author author |
dc.contributor.institution.none.fl_str_mv |
Inst Butantan Universidade de São Paulo (USP) Universidade Federal de São Paulo (UNIFESP) |
dc.contributor.author.fl_str_mv |
Ching Ching, Ana Tung Favaro, Regiane Degan Lima, Swiany Silveira Muniz Chaves, Agtha de Alencar Lima, Marcelo Andrade de [UNIFESP] Nader, Helena Bonciani [UNIFESP] Estima Abreu, Patricia A. Ho, Paulo Lee |
dc.subject.eng.fl_str_mv |
Leptospira interrogans Heparin Phage display LigB |
topic |
Leptospira interrogans Heparin Phage display LigB |
description |
LigB is an adhesin from pathogenic Leptospira that is able to bind to extracellular matrix and is considered a virulence factor. A shotgun phage display genomic library was constructed and used for panning against Heparan Sulfate Proteoglycan (HSPG). A phage clone encoding part of LigB protein was selected in panning experiments and showed specific binding to heparin. To validate the selected clone, fragments of LigB were produced as recombinant proteins and showed affinity to heparin and to mammalian cells. Heparin was also able to reduce the binding of rLB-Ct to mammalian cells. Our data suggests that the glycosaminoglycan moiety of the HSPG is responsible for its binding and could mediate the attachment of the recombinant protein rLB-Ct. Thus, heparin may act as a receptor for Leptospira to colonize and to invade the host tissue. (C) 2012 Elsevier Inc. All rights reserved. |
publishDate |
2012 |
dc.date.issued.fl_str_mv |
2012-11-02 |
dc.date.accessioned.fl_str_mv |
2016-01-24T14:27:59Z |
dc.date.available.fl_str_mv |
2016-01-24T14:27:59Z |
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 |
Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 427, n. 4, p. 774-779, 2012. |
dc.identifier.uri.fl_str_mv |
http://repositorio.unifesp.br/handle/11600/35497 http://dx.doi.org/10.1016/j.bbrc.2012.09.137 |
dc.identifier.issn.none.fl_str_mv |
0006-291X |
dc.identifier.file.none.fl_str_mv |
WOS000311134700016.pdf |
dc.identifier.doi.none.fl_str_mv |
10.1016/j.bbrc.2012.09.137 |
dc.identifier.wos.none.fl_str_mv |
WOS:000311134700016 |
identifier_str_mv |
Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 427, n. 4, p. 774-779, 2012. 0006-291X WOS000311134700016.pdf 10.1016/j.bbrc.2012.09.137 WOS:000311134700016 |
url |
http://repositorio.unifesp.br/handle/11600/35497 http://dx.doi.org/10.1016/j.bbrc.2012.09.137 |
dc.language.iso.fl_str_mv |
eng |
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eng |
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Biochemical and Biophysical Research Communications |
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http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy info:eu-repo/semantics/openAccess |
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http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy |
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openAccess |
dc.format.none.fl_str_mv |
774-779 |
dc.publisher.none.fl_str_mv |
Elsevier B.V. |
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Elsevier B.V. |
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