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Cell-Peptide Specific Interaction Can Inhibit Mycobacterium tuberculosis H37Rv Infection

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dc.creatorRodríguez, Deisy Carolinaspa
dc.creatorOcampo, Marisol
dc.creatorReyes, Cesarspa
dc.creatorArévalo?Pinzón, Gabrielaspa
dc.creatorMunoz, Marinaspa
dc.creatorPatarroyo, Manuel A.
dc.creatorPatarroyo, Manuel Elkinspa
dc.date.accessioned2020-05-25T23:55:58Z
dc.date.available2020-05-25T23:55:58Z
dc.date.created2016spa
dc.description.abstractStudying proteins from the M. tuberculosis H37Rv envelop is important for understanding host-pathogen interaction regarding bacterial infection and survival within a host; such knowledge is indispensable regarding studies aimed at developing drugs or vaccines against tuberculosis, a disease which continues to cause more than one million deaths worldwide every year. The present work presents a study of the Rv3705c protein which has been described as being an outer protein. Several servers and bioinformatics' tools were used for predicting its location on mycobacterial surface and a 3D model of the protein was obtained which was then compared to experimental circular dichroism results for its peptides. PCR assays were used for corroborating rv3705c gene presence and transcription in a laboratory strain and immunoblotting and electron microscopy were used for confirming protein localisation on cell envelop. Receptor-ligand assays revealed two peptides having high specific binding (HABPs); peptide 38485 (121DRAFHRVVDRTVGTSGQTTA140) bound to both cell lines used as infection target (U937 and A549 epithelial cell line-derived macrophages) and 38488 (181RLRENVLLQAKVTQSGNAGP200) bound to U937 cells. It was found that peptide 38485 provided significant inhibition regarding mycobacterial entry to both cell lines in in vitro assays. These results led to proposing peptide 38485 as one of the epitopes to be used in future studies aimed at characterising the immune response of functionally important synthetic peptides which could be included in developing a synthetic anti-tuberculosis vaccine. © 2015 Wiley Periodicals, Inc.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1002/jcb.25379
dc.identifier.issn07302312
dc.identifier.issn10974644
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/22280
dc.language.isoengspa
dc.publisherWiley-Liss Inc.spa
dc.relation.citationEndPage958
dc.relation.citationIssueNo. 4
dc.relation.citationStartPage946
dc.relation.citationTitleJournal of Cellular Biochemistry
dc.relation.citationVolumeVol. 117
dc.relation.ispartofJournal of Cellular Biochemistry, ISSN:07302312, 10974644, Vol.117, No.4 (2016); pp. 946-958spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84958212386&doi=10.1002%2fjcb.25379&partnerID=40&md5=ad3dc87b0a509b6b9881bdc32466f8c0spa
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.keywordRv3705c proteinspa
dc.subject.keywordBacterialeng
dc.subject.keywordSynthetic peptidespa
dc.subject.keywordUnclassified drugspa
dc.subject.keywordAntiinfective agentspa
dc.subject.keywordBacterial antigenspa
dc.subject.keywordOuter membrane proteinspa
dc.subject.keywordPeptidespa
dc.subject.keywordProtein bindingspa
dc.subject.keywordA549 cell linespa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordArticlespa
dc.subject.keywordCircular dichroismspa
dc.subject.keywordControlled studyspa
dc.subject.keywordElectron microscopyspa
dc.subject.keywordEnzyme activityspa
dc.subject.keywordGlycosylationspa
dc.subject.keywordImmune responsespa
dc.subject.keywordImmunoblottingspa
dc.subject.keywordIn vitro studyspa
dc.subject.keywordMyristylationspa
dc.subject.keywordNonhumanspa
dc.subject.keywordPolymerase chain reactionspa
dc.subject.keywordPredictionspa
dc.subject.keywordPriority journalspa
dc.subject.keywordProtein bindingspa
dc.subject.keywordProtein Data Bankspa
dc.subject.keywordProtein interactionspa
dc.subject.keywordProtein localizationspa
dc.subject.keywordProtein secondary structurespa
dc.subject.keywordTuberculosisspa
dc.subject.keywordU937 cell linespa
dc.subject.keywordWestern blottingspa
dc.subject.keywordBinding sitespa
dc.subject.keywordCell differentiationspa
dc.subject.keywordChemistryspa
dc.subject.keywordCytologyspa
dc.subject.keywordDrug effectsspa
dc.subject.keywordEpithelium cellspa
dc.subject.keywordGene expressionspa
dc.subject.keywordGenetic transcriptionspa
dc.subject.keywordGeneticsspa
dc.subject.keywordHost pathogen interactionspa
dc.subject.keywordHumanspa
dc.subject.keywordImmunologyspa
dc.subject.keywordMacrophagespa
dc.subject.keywordMicrobiologyspa
dc.subject.keywordMolecular geneticsspa
dc.subject.keywordMolecular modelspa
dc.subject.keywordMycobacterium tuberculosisspa
dc.subject.keywordPathologyspa
dc.subject.keywordSynthesisspa
dc.subject.keywordTumor cell linespa
dc.subject.keywordAmino Acid Sequencespa
dc.subject.keywordAnti-Bacterial Agentsspa
dc.subject.keywordAntigenseng
dc.subject.keywordBacterial Outer Membrane Proteinsspa
dc.subject.keywordBinding Sitesspa
dc.subject.keywordCell Differentiationspa
dc.subject.keywordCell Lineeng
dc.subject.keywordEpithelial Cellsspa
dc.subject.keywordGene Expressionspa
dc.subject.keywordHost-Pathogen Interactionsspa
dc.subject.keywordHumansspa
dc.subject.keywordMacrophagesspa
dc.subject.keywordModelseng
dc.subject.keywordMolecular Sequence Dataspa
dc.subject.keywordMycobacterium tuberculosisspa
dc.subject.keywordPeptidesspa
dc.subject.keywordProtein Bindingspa
dc.subject.keywordProtein Structureeng
dc.subject.keywordTranscriptioneng
dc.subject.keywordBIOINFORMATICSspa
dc.subject.keywordCIRCULAR DICHROISMspa
dc.subject.keywordHIGH ACTIVITY BINDING PEPTIDE (HABP)spa
dc.subject.keywordINHIBITION ASSAYspa
dc.subject.keywordRECEPTOR-LIGAND ASSAYspa
dc.titleCell-Peptide Specific Interaction Can Inhibit Mycobacterium tuberculosis H37Rv Infectionspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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