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Peptides derived from Mycobacterium tuberculosis Rv2301 protein are involved in invasion to human epithelial cells and macrophages

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dc.creatorOcampo, M.spa
dc.creatorRodríguez, D. M.spa
dc.creatorCurtidor, H.spa
dc.creatorVanegas, M.spa
dc.creatorPatarroyo, M. A.spa
dc.creatorPatarroyo, M. E.spa
dc.date.accessioned2020-05-26T00:10:36Z
dc.date.available2020-05-26T00:10:36Z
dc.date.created2012spa
dc.description.abstractThe specific function of putative cut2 protein (or CFP25), encoded by the Rv2301 gene from Mycobacterium tuberculosis H37Rv, has not been identified yet. The aim of this study was to assess some of CFP25 characteristics and its possible biological role in Mycobacterium tuberculosis H37Rv invasion process to target cells. Molecular assays indicated that the gene encoding Rv2301 is present and transcribed in M. tuberculosis complex strains. The presence of Rv2301 protein over the bacilli surface was confirmed by Western blot and immunoelectron microscopy analyses, using goats sera inoculated with synthetic peptides derived from Rv2301 protein. Receptor-ligand binding assays with carcinomic human alveolar basal epithelial cells (A549) and macrophages derived from human histolytic lymphoma monocytes (U937) allowed us to identify five high activity binding peptides (HABPs) in both cell lines, and two additional HABPs only in A549 cells. U937 HABPs binding interactions were characterized by saturation assays, finding dissociation constants (K d) within the nanomolar range and positive cooperativity (n H and gt; 1). Inhibition assays were performed to assess the possible biological role of Rv2301 identified HABPs, finding that some of them were able to inhibit invasion at a 5 ?M concentration, compared with the cytochalasin control. On the other hand, HABPs, and especially HABP 36507 located at the N-terminus of the protein, facilitated the internalization of fluorescent latex beads into A549 cells. These findings are of vital importance for the rational selection of Rv2301 HABPs, to be included as components of an antituberculosis vaccine. © 2011 Springer-Verlag.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1007/s00726-011-0938-7
dc.identifier.issn09394451
dc.identifier.issn14382199
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/24240
dc.language.isoengspa
dc.relation.citationEndPage2077
dc.relation.citationIssueNo. 6
dc.relation.citationStartPage2067
dc.relation.citationTitleAmino Acids
dc.relation.citationVolumeVol. 42
dc.relation.ispartofAmino Acids, ISSN:09394451, 14382199, Vol.42, No.6 (2012); pp. 2067-2077spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84862760198&doi=10.1007%2fs00726-011-0938-7&partnerID=40&md5=1dc0bf118b60768ae8db7b1b8d2d3886spa
dc.rights.accesRightsinfo:eu-repo/semantics/openAccess
dc.rights.accesoAbierto (Texto Completo)spa
dc.source.instnameinstname:Universidad del Rosariospa
dc.source.reponamereponame:Repositorio Institucional EdocURspa
dc.subject.keywordBacterial proteinspa
dc.subject.keywordpulmonaryeng
dc.subject.keywordCytochalasin dspa
dc.subject.keywordRv2301 proteinspa
dc.subject.keywordUnclassified drugspa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordArticlespa
dc.subject.keywordBacterial strainspa
dc.subject.keywordBinding affinityspa
dc.subject.keywordCell invasionspa
dc.subject.keywordCell surfacespa
dc.subject.keywordControlled studyspa
dc.subject.keywordDissociation constantspa
dc.subject.keywordHumanspa
dc.subject.keywordHuman cellspa
dc.subject.keywordImmunoelectron microscopyspa
dc.subject.keywordInternalizationspa
dc.subject.keywordLung alveolus epitheliumspa
dc.subject.keywordMacrophagespa
dc.subject.keywordMycobacterium tuberculosisspa
dc.subject.keywordNonhumanspa
dc.subject.keywordNucleotide sequencespa
dc.subject.keywordPriority journalspa
dc.subject.keywordProtein bindingspa
dc.subject.keywordWestern blottingspa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordAntigenseng
dc.subject.keywordBacterial proteinsspa
dc.subject.keywordBinding sitesspa
dc.subject.keywordBlottingeng
dc.subject.keywordCell lineeng
dc.subject.keywordCytochalasinsspa
dc.subject.keywordEpithelial cellsspa
dc.subject.keywordHumansspa
dc.subject.keywordKineticsspa
dc.subject.keywordMacrophagesspa
dc.subject.keywordMicroscopyeng
dc.subject.keywordMolecular sequence dataspa
dc.subject.keywordMycobacterium tuberculosisspa
dc.subject.keywordOrgan specificityspa
dc.subject.keywordPeptidesspa
dc.subject.keywordProtein bindingspa
dc.subject.keywordTuberculosiseng
dc.subject.keywordBacilli (class)spa
dc.subject.keywordCapra hircusspa
dc.subject.keywordMycobacterium tuberculosisspa
dc.subject.keywordCutinasespa
dc.subject.keywordHigh activity binding peptidesspa
dc.subject.keywordMycobacterium tuberculosisspa
dc.subject.keywordRv2301spa
dc.titlePeptides derived from Mycobacterium tuberculosis Rv2301 protein are involved in invasion to human epithelial cells and macrophagesspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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