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Anti-group A streptococcal vaccine epitope : Structure, stability, and its ability to interact with HLA class II molecules

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dc.creatorGuilherme, Luiza
dc.creatorAlba, Martha patricia
dc.creatorMoraes Ferreira, Frederico
dc.creatorEmiko Oshiro, Sandra
dc.creatorHiga, Fabio
dc.creatorPatarroyo, Manuel-Elkin
dc.creatorKalil, Jorge
dc.creator.googleGuilherme, Luizaspa
dc.creator.googleAlba, Martha Pspa
dc.creator.googleFerreira, Frederico Moraesspa
dc.creator.googleEmiko Oshiro, Sandraspa
dc.creator.googleHiga, Fabiospa
dc.creator.googlePatarroyo, Manuel Espa
dc.creator.googleKalil, Jorgespa
dc.date.accessioned2020-05-07T12:39:33Z
dc.date.available2020-05-07T12:39:33Z
dc.date.created2011
dc.date.issued2011
dc.description.abstractStreptococcus pyogenes infections remain a health problem in several countries due to poststreptococcal sequelae. We developed a vaccine epitope (StreptInCor) composed of 55 amino acids residues of the C-terminal portion of the M protein that encompasses both T and B cell protective epitopes. The nuclear magnetic resonance (NMR) structure of the StreptInCor peptide showed that the structure was composed of two microdomains linked by an 18-residue α-helix. A chemical stability study of the StreptInCor folding/unfolding process using far-UV circular dichroism showed that the structure was chemically stable with respect to pH and the concentration of urea. The T cell epitope is located in the first microdomain and encompasses 11 out of the 18 α-helix residues, whereas the B cell epitope is in the second microdomain and showed no α-helical structure. The prediction of StreptInCor epitope binding to different HLA class II molecules was evaluated based on an analysis of the 55 residues and the theoretical possibilities for the processed peptides to fit into the P1, P4, P6, and P9 pockets in the groove of several HLA class II molecules. We observed 7 potential sites along the amino acid sequence of StreptInCor that were capable of recognizing HLA class II molecules (DRB1*, DRB3*, DRB4*, and DRB5*). StreptInCor- overlapping peptides induced cellular and humoral immune responses of individuals bearing different HLA class II molecules and could be considered as a universal vaccine epitope. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1074/jbc.M110.132118
dc.identifier.issn0021-9258
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/21890
dc.language.isoengspa
dc.relation.citationEndPage6998
dc.relation.citationIssueNo. 9
dc.relation.citationStartPage6989
dc.relation.citationTitleJournal of Biological Chemistry
dc.relation.citationVolumeVol. 286
dc.relation.ispartofJournal of Biological Chemistry, ISSN: 0021-9258 Vol. 286, No. 9 (2011) pp. 6989-6998spa
dc.relation.urihttp://www.jbc.org/content/early/2010/12/17/jbc.M110.132118spa
dc.rights.accesRightsinfo:eu-repo/semantics/openAccess
dc.rights.accesoAbierto (Texto Completo)spa
dc.source.instnameinstname:Universidad del Rosario
dc.source.reponamereponame:Repositorio Institucional EdocUR
dc.subject.ddcCiencias médicas, Medicinaspa
dc.subject.ddcQuímica & ciencias afinesspa
dc.subject.keywordcontrolled studyeng
dc.subject.keywordhumaneng
dc.subject.keywordHumanseng
dc.subject.keywordAmino acid sequenceeng
dc.subject.keywordB cellseng
dc.subject.keywordClass IIeng
dc.subject.keywordHelical structureseng
dc.subject.keywordHelix residueseng
dc.subject.keywordHumoral immune responseeng
dc.subject.keywordMicro-domainseng
dc.subject.keywordMicrodomaineng
dc.subject.keywordPotential siteseng
dc.subject.keywordStreptococcus pyogeneseng
dc.subject.keywordT-cell epitopeseng
dc.subject.keywordTerminal portionseng
dc.subject.keywordUV circular dichroismeng
dc.subject.keywordAmino acidseng
dc.subject.keywordChemical stabilityeng
dc.subject.keywordDichroismeng
dc.subject.keywordMoleculeseng
dc.subject.keywordNuclear magnetic resonanceeng
dc.subject.keywordPeptideseng
dc.subject.keywordResonanceeng
dc.subject.keywordUreaeng
dc.subject.keywordVaccineseng
dc.subject.keywordAntigenseng
dc.subject.keywordAmino acideng
dc.subject.keywordEpitopeeng
dc.subject.keywordHLA antigen class 2eng
dc.subject.keywordHLA DR antigeneng
dc.subject.keywordM proteineng
dc.subject.keywordPeptideeng
dc.subject.keywordStreptincoreng
dc.subject.keywordStreptococcus vaccineeng
dc.subject.keywordUnclassified drugeng
dc.subject.keywordUreaeng
dc.subject.keywordAlpha helixeng
dc.subject.keywordAlpha helixeng
dc.subject.keywordAmino acid sequenceeng
dc.subject.keywordAntigen bindingeng
dc.subject.keywordAntigen recognitioneng
dc.subject.keywordArticleeng
dc.subject.keywordCarboxy terminal sequenceeng
dc.subject.keywordCellular immunityeng
dc.subject.keywordCircular dichroismeng
dc.subject.keywordHuman tissueeng
dc.subject.keywordHumoral immunityeng
dc.subject.keywordMolecular interactioneng
dc.subject.keywordMolecular stabilityeng
dc.subject.keywordNuclear magnetic resonanceeng
dc.subject.keywordpHeng
dc.subject.keywordPredictioneng
dc.subject.keywordPriority journaleng
dc.subject.keywordProtein domaineng
dc.subject.keywordProtein foldingeng
dc.subject.keywordProtein structureeng
dc.subject.keywordStreptococcus pyogeneseng
dc.subject.keywordAntigen Presentationeng
dc.subject.keywordEpitopeseng
dc.subject.keywordEpitopeseng
dc.subject.keywordHistocompatibility Antigens Class IIeng
dc.subject.keywordNuclear Magnetic Resonanceeng
dc.subject.keywordProtein Stabilityeng
dc.subject.keywordProtein Structureeng
dc.subject.keywordProtein Structureeng
dc.subject.keywordStreptococcal Infectionseng
dc.subject.keywordStreptococcal Vaccineseng
dc.subject.keywordStreptococcus pyogeneseng
dc.titleAnti-group A streptococcal vaccine epitope : Structure, stability, and its ability to interact with HLA class II moleculesspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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