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dc.creatorSalazar, Luz M. 
dc.creatorAlba, Martha P. 
dc.creatorCurtidor, Hernando 
dc.creatorBermudez, Adriana 
dc.creatorVargas, Luis E. 
dc.creatorRivera, Zuly J. 
dc.creatorPatarroyo, Manuel E. 
dc.date.accessioned2020-08-06T16:20:30Z
dc.date.available2020-08-06T16:20:30Z
dc.date.created2004-09-10
dc.identifier.issnISSN: 0006-291X
dc.identifier.issnEISSN: 1090-2104
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/26036
dc.description.abstractThe Plasmodium falciparum acidic–basic repeat antigen represents a potential malarial vaccine candidate. One of this protein’s high activity binding peptides, named 2150 (161KMNMLKENVDYIQKNQNLFK180), is conserved, non-immunogenic, and non-protection-inducing. Analogue peptides whose critical binding residues (in bold) were replaced by amino-acids having similar mass but different charge were synthesized and tested to try to modify such immunological properties. These analogues’ HLA-DR?1* molecule binding ability were also studied in an attempt to explain their biological mechanisms and correlate binding capacity and immunological function with their three-dimensional structure determined by 1H NMR. A 310 distorted helical structure was identified in protective and immunogenic peptide 24922 whilst ?-helical structure was found for non-immunogenic, non-protective peptides having differences in ?-helical position. The changes performed on immunogenic, protection-inducing peptide 24922 allowed it to bind specifically to the HLA-DR?1*0301 molecule, suggesting that these changes may lead to better interaction with the MHC Class II-peptide-TCR complex rendering it immunogenic and protective, thus suggesting a new way of developing multi-component, sub-unit-based anti-malarial vaccines.
dc.format.mimetypeapplication/pdf
dc.language.isoeng
dc.relation.ispartofBiochemical and Biophysical Research Communications, ISSN: 0006-291X;EISSN: 1090-2104, Vol.332, No.1 (2004); pp.119-125
dc.relation.urihttps://www.sciencedirect.com/science/article/abs/pii/S0006291X04015803?via%3Dihub
dc.sourceBiochemical and Biophysical Research Communications
dc.titleChanging ABRA protein peptide to fit into the HLA-DRbeta1*0301 molecule renders it protection-inducing
dc.typearticle
dc.publisherElsevier
dc.subject.keywordABRA protein
dc.subject.keywordPeptide analogues
dc.subject.keywordVaccine candidate
dc.subject.keywordMalaria
dc.subject.keywordConformation
dc.subject.keywordNMR
dc.rights.accesRightsinfo:eu-repo/semantics/restrictedAccess
dc.type.spaArtículo
dc.rights.accesoRestringido (Acceso a grupos específicos)
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.identifier.doihttps://doi.org/10.1016/j.bbrc.2004.07.086
dc.title.TranslatedTitleCambiar el péptido de la proteína ABRA para que se ajuste a la molécula HLA-DRbeta1 * 0301 hace que induzca la protección
dc.relation.citationEndPage125
dc.relation.citationIssueNo. 1
dc.relation.citationStartPage119
dc.relation.citationTitleBiochemical and Biophysical Research Communications
dc.relation.citationVolumeVol. 332


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