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Orientating peptide residues and increasing the distance between Pockets to enable fitting into MHC-TCR complex determine protection against malaria.

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dc.creatorCifuentes, Gladysspa
dc.creatorEspejo, Fabiolaspa
dc.creatorVargas, Luis Eduardospa
dc.creatorParra, Carlosspa
dc.creatorVanegas, Magnoliaspa
dc.creatorPatarroyo, Manuel Elkinspa
dc.date.accessioned2020-08-06T16:21:38Z
dc.date.available2020-08-06T16:21:38Z
dc.date.created2004-05-06spa
dc.description.abstractThe erythrocyte binding antigen EBA-175 is a 175-kDa Plasmodium falciparum protein, which has been shown to be involved in the process of invasion of erythrocytes. It has been found that conserved peptide 1818 belonging to this protein has high red blood cell binding capacity and plays an important role in the invasion process. This peptide is neither immunogenic nor protective. Peptide 1818 analogues had some of their previously recognized critical red blood cell binding residues substituted for amino acids having similar volume or mass but different polarity to make them fit into HLA-DR?1*1101 molecules; these 1818 peptide analogues were then synthesized and inoculated into Aotus nancymaae monkeys, generating different immunogenic and/or protective immune responses. Short structures such as 310-helix, classical, or distorted type-III ?-turns were found in the immunogenic and protective peptides once the secondary structure had been analyzed by NMR and its structure correlated with its immunological properties. These data suggest that peptide flexibility may lead to better fitting into immune system molecules, therefore making them excellent candidates for consideration as components of a subunit-based, multicomponent synthetic antimalarial vaccine.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1021/bi049698%2B
dc.identifier.issnISSN: 0006-2960
dc.identifier.issnEISSN: 1520-4995
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/26417
dc.language.isoengspa
dc.publisherACS Publicationsspa
dc.relation.citationEndPage6553
dc.relation.citationIssueNo. 21
dc.relation.citationStartPage6545
dc.relation.citationTitleBiochemistry
dc.relation.citationVolumeVol. 43
dc.relation.ispartofBiochemistry, ISSN: 0006-2960;EISSN: 1520-4995, Vol.43, No.21(May, 2013) pp.6545–6553spa
dc.relation.urihttps://pubs.acs.org/doi/pdf/10.1021/bi049698%2Bspa
dc.rights.accesRightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.accesoRestringido (Acceso a grupos específicos)spa
dc.sourceBiochemistryspa
dc.source.instnameinstname:Universidad del Rosario
dc.source.reponamereponame:Repositorio Institucional EdocUR
dc.subject.keywordChemical structurespa
dc.subject.keywordPeptides and proteinsspa
dc.subject.keywordMonomersspa
dc.subject.keywordParasitesspa
dc.subject.keywordMoleculesspa
dc.titleOrientating peptide residues and increasing the distance between Pockets to enable fitting into MHC-TCR complex determine protection against malaria.spa
dc.title.TranslatedTitleOrientar los residuos de péptidos y aumentar la distancia entre los bolsillos para permitir el ajuste en el complejo MHC-TCR determina la protección contra la malaria.spa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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