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Expression and purification of human respiratory syncytial virus recombinant fusion protein

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dc.contributor.authorArcuri, Helen A. [UNESP]
dc.contributor.authorApponi, Luciano H. [UNESP]
dc.contributor.authorValentini, Sandro Roberto [UNESP]
dc.contributor.authorDurigon, Edison L.
dc.contributor.authorAzevedo, Walter F. de
dc.contributor.authorFossey, Marcelo Andrés [UNESP]
dc.contributor.authorRahal, Paula [UNESP]
dc.contributor.authorde Souza, Fatima P. [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionPontifícia Universidade Católica do Rio Grande do Sul (PUCRS)
dc.date.accessioned2014-05-20T14:00:30Z
dc.date.available2014-05-20T14:00:30Z
dc.date.issued2008-12-01
dc.description.abstractThe Human Respiratory Syncytial Virus (HRSV) fusion protein (F) was expressed in Escherichia call BL21A using the pET28a vector at 37 degrees C. The protein was purified from the soluble fraction using affinity resin. The structural quality of the recombinant fusion protein and the estimation of its secondary structure were obtained by circular dichroism. Structural models of the fusion protein presented 46% of the helices in agreement with the spectra by circular dichroism analysis. There are only few studies that succeeded in expressing the HRSV fusion protein in bacteria. This is a report on human fusion protein expression in E. call and structure analysis, representing a step forward in the development of fusion protein F inhibitors and the production of antibodies. (c) 2008 Elsevier B.V. All rights reserved.en
dc.description.affiliationUNESP, Inst Biociencias Letras & Ciencias Exatas, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUNESP, Fac Ciencias Farmaceut, BR-14801902 Araraquara, SP, Brazil
dc.description.affiliationUniv São Paulo, Inst Ciencias Biomed, BR-05508900 São Paulo, Brazil
dc.description.affiliationPUCRGS, Fac Ciencias Biol, BR-90619900 Porto Alegre, RS, Brazil
dc.description.affiliationUnespUNESP, Inst Biociencias Letras & Ciencias Exatas, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUnespUNESP, Fac Ciencias Farmaceut, BR-14801902 Araraquara, SP, Brazil
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipIdFAPESP: 02/08461-2
dc.description.sponsorshipIdCNPq: 150358/2003-2
dc.format.extent146-152
dc.identifierhttp://dx.doi.org/10.1016/j.pep.2008.08.005
dc.identifier.citationProtein Expression and Purification. San Diego: Academic Press Inc. Elsevier B.V., v. 62, n. 2, p. 146-152, 2008.
dc.identifier.doi10.1016/j.pep.2008.08.005
dc.identifier.issn1046-5928
dc.identifier.lattes7991082362671212
dc.identifier.lattes4101562077663619
dc.identifier.orcid0000-0001-5693-6148
dc.identifier.urihttp://hdl.handle.net/11449/21402
dc.identifier.wosWOS:000260598900002
dc.language.isoeng
dc.publisherAcademic Press Inc. Elsevier B.V.
dc.relation.ispartofProtein Expression and Purification
dc.relation.ispartofjcr1.338
dc.relation.ispartofsjr0,648
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectFusion proteinen
dc.subjectPurificationen
dc.subjectDichroism analysisen
dc.subjectMolecular modelingen
dc.subjectExpressionen
dc.titleExpression and purification of human respiratory syncytial virus recombinant fusion proteinen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderAcademic Press Inc. Elsevier B.V.
dspace.entity.typePublication
unesp.author.lattes7991082362671212[7]
unesp.author.lattes4101562077663619
unesp.author.orcid0000-0002-2012-388X[6]
unesp.author.orcid0000-0001-5693-6148[7]
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Biociências, Letras e Ciências Exatas, São José do Rio Pretopt
unesp.departmentBiologia - IBILCEpt
unesp.departmentFísica - IBILCEpt

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São José do Rio Preto - IBILCE - Instituto de Biociências, Letras e Ciências Exatas