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In silico and in vitro analysis of boAP3d1 protein interaction with bovine leukaemia virus gp51

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dc.creatorCorredor Figueroa, Adriana Patricia
dc.creatorGonzalez, Janneth
dc.creatorBaquero, Luis Alfredo
dc.creatorCurtidor, Hernando
dc.creatorOlaya-Galan, Nury-Nathalia
dc.creatorPatarroyo, Manuel A.
dc.creatorGutiérrez, María Fernanda
dc.creator.googleCorredor, Adriana Patricia
dc.creator.googleGonzález, Janneth
dc.creator.googleBaquero, Luis Alfredo
dc.creator.googleCurtidor, Hernando
dc.creator.googleOlaya-Galán, Nury Nathalia
dc.creator.googlePatarroyo, Manuel Alfonso
dc.creator.googleGutiérrez, María Fernanda
dc.date.accessioned2019-09-23T16:15:06Z
dc.date.available2019-09-23T16:15:06Z
dc.date.created2018
dc.date.issued2018-06-21
dc.description.abstractThe envelope glycoprotein 51 (gp51) is essential for bovine leukaemia virus (BLV) entry to bovine B-lymphocytes. Although the bovine adaptor protein 3 complex subunit delta-1 (boAP3D1) has been proposed as the potential receptor, the specific ligand-receptor interaction has not yet been completely defined and boAP3D1 receptor and gp51 3D structures have not been determined. This study was thus aimed at a functional annotation of boAP3D1 cellular adaptor protein and BLV gp51 and, proposing a reliable model for gp51-AP3D1 interaction using bioinformatics tools. The boAP3D1 receptor interaction patterns were calculated based on models of boAP3D1 receptor and gp51 complexes’ 3D structures, which were constructed using homology techniques and data-driven docking strategy. The results showed that the participation of 6 key amino acids (aa) on gp51 (Asn170, Trp127, His115, Ala97, Ser98 and Glu128) and 4 aa on AP3D1 (Lys925, Asp807, Asp695 and Arg800) was highly probable in the interaction between gp51 and BLVR domains. Three gp51 recombinant peptides were expressed and purified to validate these results: the complete domain (rgp51), the N-terminal portion (rNgp51) and the C-terminal fragment (rCgp51); and binding assays to Madin-Darby bovine kidney (MDBK) cells were then carried out with each recombinant. It was found that rNgp51 preferentially bound to MDBK cells, suggesting this domain’s functional role during invasion. The rNgp51-MDBK cell interaction was sensitive to trypsin (98% reduction) and chymotrypsin treatment (80% reduction). These results highlighted that the N-terminal portion of gp51 interacted in vitro with the AP3D1 receptor and provides a plausible in silico interaction model. © 2018 Corredor et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1371/journal.pone.0199397
dc.identifier.issn1932-6203
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/20317
dc.language.isoengspa
dc.relation.citationTitlePLoS ONE
dc.relation.citationVolumeVol. 13
dc.relation.ispartofPLoS ONE, ISSN:1932-6203, Vol. 13 (2018)spa
dc.relation.urihttps://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0199397&type=printablespa
dc.rights.accesRightsinfo:eu-repo/semantics/openAccess
dc.rights.accesoAbierto (Texto Completo)spa
dc.source.bibliographicCitation(2017) International Committee on Taxonomy of Viruses, , ICTVspa
dc.source.instnameinstname:Universidad del Rosario
dc.source.reponamereponame:Repositorio Institucional EdocUR
dc.subjectProteína adaptadoraspa
dc.subjectAlaninaspa
dc.subjectArgininaspa
dc.subjectAsparaginaspa
dc.subjectÁcido aspárticospa
dc.subjectProteína Boap3D1spa
dc.subjectQuimotripsinaspa
dc.subjectÁcido glutamicospa
dc.subjectGlicoproteína 5spa
dc.subjectHistidinaspa
dc.subjectLisinaspa
dc.subjectSerinaspa
dc.subjectTripsinaspa
dc.subjectTriptófanospa
dc.subjectMedicamento no clasificadospa
dc.subjectGlicoproteína viralspa
dc.subjectSecuencia amino terminalspa
dc.subjectSitio de uniónspa
dc.subjectBioinformáticaspa
dc.subjectVirus de la leucemia bovinaspa
dc.subjectSecuencia terminal carboxispa
dc.subjectInteracción celularspa
dc.subjectFormación complejaspa
dc.subjectEstudio controladospa
dc.subjectEstudio in vitrospa
dc.subjectlínea celular mdbkspa
dc.subjectAcoplamiento molecularspa
dc.subjectNo humanospa
dc.subjectEnlace proteicospa
dc.subjectDominio de proteínasspa
dc.subjectExpresión de proteínasspa
dc.subjectInteracción Proteína Proteínaspa
dc.subject.ddcProducción animal (Zootecnia)spa
dc.subject.keywordArticlespa
dc.subject.keywordAdaptor Proteineng
dc.subject.keywordAlanineeng
dc.subject.keywordArginineeng
dc.subject.keywordAsparagineeng
dc.subject.keywordAspartic Acideng
dc.subject.keywordBoap3D1 Proteineng
dc.subject.keywordSerineeng
dc.subject.keywordChymotrypsineng
dc.subject.keywordGlutamic Acideng
dc.subject.keywordGlycoprotein 5eng
dc.subject.keywordLysineeng
dc.subject.keywordHistidineeng
dc.subject.keywordTrypsineng
dc.subject.keywordTryptophaneng
dc.subject.keywordUnclassified Drugeng
dc.subject.keywordVirus Glycoproteineng
dc.subject.keywordAmino Terminal Sequenceeng
dc.subject.keywordBinding Siteeng
dc.subject.keywordBioinformaticseng
dc.subject.keywordBovine Leukemia Viruseng
dc.subject.keywordCarboxy Terminal Sequenceeng
dc.subject.keywordCell Interactioneng
dc.subject.keywordComplex Formationeng
dc.subject.keywordControlled Studyeng
dc.subject.keywordIn Vitro Studyeng
dc.subject.keywordMdbk Cell Lineeng
dc.subject.keywordMolecular Dockingeng
dc.subject.keywordNonhumaneng
dc.subject.keywordProtein Bindingeng
dc.subject.keywordProtein Domaineng
dc.subject.keywordProtein Expressioneng
dc.subject.keywordProtein Protein Interactioneng
dc.subject.lembLeucemia bovinaspa
dc.subject.lembQuimotripsinaspa
dc.titleIn silico and in vitro analysis of boAP3d1 protein interaction with bovine leukaemia virus gp51spa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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