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Atomic fidelity of subunit-based chemically-synthesized antimalarial vaccine components

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dc.creatorPatarroyo, Manuel E.spa
dc.creatorCifuentes, Gladysspa
dc.creatorMartínez, Nora L.spa
dc.creatorPatarroyo, Manuel A.spa
dc.date.accessioned2020-05-25T23:58:33Z
dc.date.available2020-05-25T23:58:33Z
dc.date.created2010spa
dc.description.abstractThe tri-dimensional (3D) structure determined by NMR of functionally relevant High Activity Binding Peptides (HABPs) of chemically-synthesized malarial proteins, involved in invasion to target cells, is practically identical, at the atomic level, to their corresponding recombinantly produced proteins, determined by X-ray crystallography. Both recombinant proteins as well as these chemically-synthesized HABPs bind to host-cell receptors through channels or troughs formation, stabilized by hydrogen bonding; most of them are located on distant segments to the highly polymorphic, highly antigenic, strain specific amino acid sequences the parasite uses to evade immune pressure. When these immunologically silent conserved HABPs are specifically modified, they become highly immunogenic and capable of inducing protective immune responses, supporting the specifically modified minimal subunit-based, multiepitopic, chemically-synthesized vaccines concept. © 2009 Elsevier Ltd. All rights reserved.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1016/j.pbiomolbio.2009.10.006
dc.identifier.issn796107
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/22886
dc.language.isoengspa
dc.relation.citationEndPage44
dc.relation.citationIssueNo. 1
dc.relation.citationStartPage38
dc.relation.citationTitleProgress in Biophysics and Molecular Biology
dc.relation.citationVolumeVol. 102
dc.relation.ispartofProgress in Biophysics and Molecular Biology, ISSN:796107, Vol.102, No.1 (2010); pp. 38-44spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-76349093367&doi=10.1016%2fj.pbiomolbio.2009.10.006&partnerID=40&md5=f5879cd1135c161e08bd794cb5c071d8spa
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.keywordAntimalarial agentspa
dc.subject.keywordfalciparumeng
dc.subject.keywordAnimalspa
dc.subject.keywordChemistryspa
dc.subject.keywordDrug effectspa
dc.subject.keywordImmunologyspa
dc.subject.keywordMalaria falciparumspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordReviewspa
dc.subject.keywordSynthesisspa
dc.subject.keywordAnimalsspa
dc.subject.keywordAntimalarialsspa
dc.subject.keywordMalariaeng
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordVaccinesspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordChemically-synthesized vaccinesspa
dc.subject.keywordHla-dr?1* moleculesspa
dc.subject.keywordMalariaspa
dc.subject.keywordMhc ii-peptide-tcr complexspa
dc.subject.keywordPlasmodium falciparumspa
dc.titleAtomic fidelity of subunit-based chemically-synthesized antimalarial vaccine componentsspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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