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Mycobacterium tuberculosis PE9 protein has high activity binding peptides which inhibit target cell invasion

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dc.creatorDíaz D.P.spa
dc.creatorOcampo M.spa
dc.creatorPabón L.spa
dc.creatorHerrera C.spa
dc.creatorPatarroyo M.A.spa
dc.creatorMunoz M.spa
dc.creatorPatarroyo M.E.spa
dc.date.accessioned2020-05-26T00:11:49Z
dc.date.available2020-05-26T00:11:49Z
dc.date.created2016spa
dc.description.abstractPE/PPE proteins are involved in several processes during Mycobacterium tuberculosis (Mtb) infection of target cells; studying them is extremely interesting as they are the only ones from the Mycobacterium genus, they abound in pathogenic species such as Mtb and their function remains yet unknown. The PE9 protein (Rv1088) was characterised, the rv1088 gene was identified by PCR in Mtb complex strains and its expression and localisation on mycobacterial surface was confirmed by Western blot and immunoelectron microscopy. Bioinformatics tools were used for predicting PE9 protein structural aspects and experimental study involved the circular dichroism of synthetic peptides. The peptides were tested in binding assays involving U937 and A549 cells; two high activity binding peptides (HABPs) were found for both cell lines (39226-1MSYMIATPAALTAAATDIDGI21 and 39232-125YQRHFGTGGQPEFRQHSEHRR144), one for U937 (39231-104YAGAGRRQRRRRSGDGQWRLRQ124) and one for A549 (39230-83YGTGVFRRRRGRQTVTAAEHRA103). HABP 39232 inhibited mycobacterial entry to A549 cells (~70%) and U937 cells (~50%), peptides 39226 and 39231 inhibited entry to U937 cells (~60% and 80%, respectively) and peptide 39230 inhibited entry to A549 cells (~60%). This emphasised HABPs' functional importance in recognition between Mtb H37Rv and target cell receptors. These peptide sequences could be involved in invasion and were recognised by the host's immune system, thereby highlighting their use when designing an efficient anti-tuberculosis multiantigenic vaccine. © 2016 Elsevier B.V.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1016/j.ijbiomac.2015.12.081
dc.identifier.issn1418130
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/24335
dc.language.isoengspa
dc.publisherElsevier B.V.spa
dc.relation.citationEndPage655
dc.relation.citationStartPage646
dc.relation.citationTitleInternational Journal of Biological Macromolecules
dc.relation.citationVolumeVol. 86
dc.relation.ispartofInternational Journal of Biological Macromolecules, ISSN:1418130, Vol.86,(2016); pp. 646-655spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84957990000&doi=10.1016%2fj.ijbiomac.2015.12.081&partnerID=40&md5=c32fb67debabb348643df423c116c4ecspa
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.keywordmoleculareng
dc.subject.keywordUnclassified drugspa
dc.subject.keywordBacterial proteinspa
dc.subject.keywordPeptidespa
dc.subject.keywordProtein bindingspa
dc.subject.keywordArticlespa
dc.subject.keywordBacterial strainspa
dc.subject.keywordCell invasionspa
dc.subject.keywordCircular dichroismspa
dc.subject.keywordControlled studyspa
dc.subject.keywordCrystal structurespa
dc.subject.keywordMycobacterium tuberculosisspa
dc.subject.keywordNonhumanspa
dc.subject.keywordProtein bindingspa
dc.subject.keywordProtein expressionspa
dc.subject.keywordProtein localizationspa
dc.subject.keywordProtein secondary structurespa
dc.subject.keywordProtein targetingspa
dc.subject.keywordSurface propertyspa
dc.subject.keywordA-549 cell linespa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordBiologyspa
dc.subject.keywordChemistryspa
dc.subject.keywordEnzyme specificityspa
dc.subject.keywordEpithelium cellspa
dc.subject.keywordGenetic transcriptionspa
dc.subject.keywordGeneticsspa
dc.subject.keywordHumanspa
dc.subject.keywordMacrophagespa
dc.subject.keywordMetabolismspa
dc.subject.keywordMicrobiologyspa
dc.subject.keywordMolecular modelspa
dc.subject.keywordMycobacterium tuberculosisspa
dc.subject.keywordPhysiologyspa
dc.subject.keywordProtein conformationspa
dc.subject.keywordProtein transportspa
dc.subject.keywordA549 cellsspa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordBacterial proteinsspa
dc.subject.keywordComputational biologyspa
dc.subject.keywordEpithelial cellsspa
dc.subject.keywordHumansspa
dc.subject.keywordMacrophagesspa
dc.subject.keywordModelseng
dc.subject.keywordMycobacterium tuberculosisspa
dc.subject.keywordPeptidesspa
dc.subject.keywordProtein bindingspa
dc.subject.keywordProtein conformationspa
dc.subject.keywordProtein transportspa
dc.subject.keywordSubstrate specificityspa
dc.subject.keywordTranscriptioneng
dc.subject.keywordPe9 proteinspa
dc.subject.keywordSynthetic peptidespa
dc.subject.keywordTuberculosisspa
dc.titleMycobacterium tuberculosis PE9 protein has high activity binding peptides which inhibit target cell invasionspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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