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Electrostatic potential as a tool to understand interactions between malaria vaccine candidate peptides and MHC II molecules

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dc.creatorAgudelo W.A.spa
dc.creatorGalindo J.F.spa
dc.creatorPatarroyo M.E.spa
dc.date.accessioned2020-05-26T00:02:38Z
dc.date.available2020-05-26T00:02:38Z
dc.date.created2011spa
dc.description.abstractOne of the most important problems in vaccine development consists in understanding receptor-ligand interactions between Class II Major Histocompatibility Complex molecules (MHC II) and antigenic peptides involved in inducing an appropriate immune response. In this study, we used X-ray crystallography structural data provided by the HLA-DR?1*0301-CLIP peptide interaction to compare native non-immunogenic and specifically-modified immunogenic peptides derived from the malarial SALSA protein, by analyzing molecular electrostatic potential surfaces on the most important regions of the peptide binding groove (Pockets 1, 4, 6 and 9). Important differences were found on the electrostatic potential induced by these peptides, particularly in MHC II conserved residues: Q?9, S?53, N?62, N?69, Y?30, Y?60, W?61, Q?70, K?71 and V?86, the same ones involved in establishing hydrogen bonds between Class II molecule-peptide and the recognition by T cell receptor, it correlating well with the change in their immunological properties.The results clearly suggest that modifications done on the electrostatic potential of these amino acids could favor the induction of different immune responses and therefore, their identification could allow modifying peptides a priori and in silico, so as to render them into immunogenic and protection-inducers and hence suitable components of a chemically-synthesized, multi-antigenic, minimal subunit based vaccine. © 2011 Elsevier Inc.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1016/j.bbrc.2011.05.145
dc.identifier.issn0006291X
dc.identifier.issn10902104
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/23509
dc.language.isoengspa
dc.relation.citationEndPage415
dc.relation.citationIssueNo. 3
dc.relation.citationStartPage410
dc.relation.citationTitleBiochemical and Biophysical Research Communications
dc.relation.citationVolumeVol. 410
dc.relation.ispartofBiochemical and Biophysical Research Communications, ISSN:0006291X, 10902104, Vol.410, No.3 (2011); pp. 410-415spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-79960048690&doi=10.1016%2fj.bbrc.2011.05.145&partnerID=40&md5=f235f2a950912eaf538c91c4db5dc535spa
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.keywordHLA DR1 antigenspa
dc.subject.keywordMajor histocompatibility antigen class 2spa
dc.subject.keywordMalaria vaccinespa
dc.subject.keywordSALSA proteinspa
dc.subject.keywordT lymphocyte receptorspa
dc.subject.keywordUnclassified drugspa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordArticlespa
dc.subject.keywordHydrogen bondspa
dc.subject.keywordImmune responsespa
dc.subject.keywordImmunogenicityspa
dc.subject.keywordPriority journalspa
dc.subject.keywordStatic electricityspa
dc.subject.keywordX ray crystallographyspa
dc.subject.keywordAmino Acid Sequencespa
dc.subject.keywordCrystallographyeng
dc.subject.keywordHistocompatibility Antigens Class IIspa
dc.subject.keywordHLA-DR Antigensspa
dc.subject.keywordHumansspa
dc.subject.keywordMalaria Vaccinesspa
dc.subject.keywordMolecular Sequence Dataspa
dc.subject.keywordPeptidesspa
dc.subject.keywordProtein Conformationspa
dc.subject.keywordStatic Electricityspa
dc.subject.keywordHLA-dr?1*0301spa
dc.subject.keywordMalariaspa
dc.subject.keywordMolecular electrostatic potentialspa
dc.subject.keywordReceptor-ligand interactionspa
dc.subject.keywordSALSAspa
dc.titleElectrostatic potential as a tool to understand interactions between malaria vaccine candidate peptides and MHC II moleculesspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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