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Atomic evidence that modification of H-bonds established with amino acids critical for host-cell binding induces sterile immunity against malaria

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dc.creatorPatarroyo, Manuel E.spa
dc.creatorCifuentes, Gladysspa
dc.creatorPiraján, Camilospa
dc.creatorMoreno-Vranich, Armandospa
dc.creatorVanegas, Magnolia
dc.date.accessioned2020-05-26T00:02:37Z
dc.date.available2020-05-26T00:02:37Z
dc.date.created2010spa
dc.description.abstractBased on the 3D X-ray crystallographic structures of relevant proteins of the malaria parasite involved in invasion to host cells and 3D NMR structures of High Activity Binding Peptides (HABPs) and their respective analogues, it was found that HABPs are rendered into highly immunogenic and sterile immunity inducers in the Aotus experimental model by modifying those amino acids that establish H-bonds with other HABPs or binding to host's cells. This finding adds striking and novel physicochemical principles, at the atomic level, for a logical and rational vaccine development methodology against infectious disease, among them malaria. © 2010 Elsevier Inc. All rights reserved.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1016/j.bbrc.2010.03.004
dc.identifier.issn0006291X
dc.identifier.issn10902104
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/23507
dc.language.isoengspa
dc.relation.citationEndPage535
dc.relation.citationIssueNo. 3
dc.relation.citationStartPage529
dc.relation.citationTitleBiochemical and Biophysical Research Communications
dc.relation.citationVolumeVol. 394
dc.relation.ispartofBiochemical and Biophysical Research Communications, ISSN:0006291X, 10902104, Vol.394, No.3 (2010); pp. 529-535spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-77950517324&doi=10.1016%2fj.bbrc.2010.03.004&partnerID=40&md5=81f947136ff0a7d59323b1ed3dcd4001spa
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.keywordMalaria vaccinespa
dc.subject.keywordx-rayeng
dc.subject.keywordAmino acid compositionspa
dc.subject.keywordAnimal experimentspa
dc.subject.keywordAnimal modelspa
dc.subject.keywordAotusspa
dc.subject.keywordArticlespa
dc.subject.keywordControlled studyspa
dc.subject.keywordHost resistancespa
dc.subject.keywordHydrogen bondspa
dc.subject.keywordImmunogenicityspa
dc.subject.keywordMalaria falciparumspa
dc.subject.keywordNonhumanspa
dc.subject.keywordPhysical chemistryspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordPriority journalspa
dc.subject.keywordVaccine productionspa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordAnimalsspa
dc.subject.keywordAntibodieseng
dc.subject.keywordAntigenseng
dc.subject.keywordAotus trivirgatusspa
dc.subject.keywordCrystallographyeng
dc.subject.keywordHost-parasite interactionsspa
dc.subject.keywordHydrogen bondingspa
dc.subject.keywordMalariaspa
dc.subject.keywordMalaria vaccinesspa
dc.subject.keywordMolecular sequence dataspa
dc.subject.keywordNuclear magnetic resonanceeng
dc.subject.keywordPeptidesspa
dc.subject.keywordProtein conformationspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordH-bondsspa
dc.subject.keywordMalariaspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordSterile immunityspa
dc.titleAtomic evidence that modification of H-bonds established with amino acids critical for host-cell binding induces sterile immunity against malariaspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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