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Redefining an epitope of a malaria vaccine candidate, with antibodies against the N-terminal MSA-2 antigen of Plasmodium harboring non-natural peptide bonds

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dc.creatorLozano, José Manuelspa
dc.creatorGuerrero, Yuly Andreaspa
dc.creatorAlba, Martha Patriciaspa
dc.creatorLesmes, Liliana Patriciaspa
dc.creatorEscobar, José Oswaldospa
dc.creatorPatarroyo, Manuel Elkinspa
dc.date.accessioned2020-05-26T00:10:59Z
dc.date.available2020-05-26T00:10:59Z
dc.date.created2013spa
dc.description.abstractThe aim of obtaining novel vaccine candidates against malaria and other transmissible diseases can be partly based on selecting non-polymorphic peptides from relevant antigens of pathogens, which have to be then precisely modified for inducing a protective immunity against the disease. Bearing in mind the high degree of the MSA-221-40 peptide primary structure's genetic conservation among malaria species, and its crucial role in the high RBC binding ability of Plasmodium falciparum (the main agent causing malaria), structurally defined probes based on non-natural peptide-bond isosteres were thus designed. Thus, two peptide mimetics were obtained (so-called reduced amide pseudopeptides), in which naturally made amide bonds of the 30FIN32-binding motif of MSA-2 were replaced with ?-[CH2-NH] methylene amide isostere bonds, one between the F-I and the second between I-N amino acid pairs, respectively, coded as ?-128 ?-130. These peptide mimetics were used to produce poly- and monoclonal antibodies in Aotus monkeys and BALB/c mice. Parent reactive mice-derived IgM isotype cell clones were induced to Ig isotype switching to IgG sub-classes by controlled in vitro immunization experiments. These mature isotype immunoglobulins revealed a novel epitope in the MSA-225-32 antigen and two polypeptides of rodent malaria species. Also, these antibodies' functional activity against malaria was tested by in vitro assays, demonstrating high efficacy in controlling infection and evidencing neutralizing capacity for the rodent in vivo malaria infection. The neutralizing effect of antibodies induced by site-directed designed peptide mimetics on Plasmodium's biological development make these pseudopeptides a valuable tool for future development of immunoprophylactic strategies for controlling malarial infection. © 2013 The Author(s).eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1007/s00726-013-1541-x
dc.identifier.issn09394451
dc.identifier.issn14382199
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/24274
dc.language.isoengspa
dc.relation.citationEndPage935
dc.relation.citationIssueNo. 4
dc.relation.citationStartPage913
dc.relation.citationTitleAmino Acids
dc.relation.citationVolumeVol. 45
dc.relation.ispartofAmino Acids, ISSN:09394451, 14382199, Vol.45, No.4 (2013); pp. 913-935spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84885297133&doi=10.1007%2fs00726-013-1541-x&partnerID=40&md5=f89e180b9d947a30d5c4e088650d9093spa
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.keywordEpitopespa
dc.subject.keywordmonoclonaleng
dc.subject.keywordImmunoglobulin classspa
dc.subject.keywordMalaria vaccinespa
dc.subject.keywordMerozoite surface protein 2spa
dc.subject.keywordMonoclonal antibodyspa
dc.subject.keywordPeptidomimetic agentspa
dc.subject.keywordPolyclonal antibodyspa
dc.subject.keywordAnimal cellspa
dc.subject.keywordAnimal experimentspa
dc.subject.keywordAnimal modelspa
dc.subject.keywordAotusspa
dc.subject.keywordArticlespa
dc.subject.keywordBagg albino mousespa
dc.subject.keywordBioinformaticsspa
dc.subject.keywordChemical structurespa
dc.subject.keywordControlled studyspa
dc.subject.keywordEpitope mappingspa
dc.subject.keywordErythrocytespa
dc.subject.keywordFemalespa
dc.subject.keywordInfrared spectroscopyspa
dc.subject.keywordMousespa
dc.subject.keywordNonhumanspa
dc.subject.keywordParasitemiaspa
dc.subject.keywordPassive immunizationspa
dc.subject.keywordPeptide synthesisspa
dc.subject.keywordPlasmodiumspa
dc.subject.keywordPlasmodium bergheispa
dc.subject.keywordPlasmodium berghei infectionspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordPlasmodium yoeliispa
dc.subject.keywordPlasmodium yoelii infectionspa
dc.subject.keywordPriority journalspa
dc.subject.keywordProton nuclear magnetic resonancespa
dc.subject.keywordSolid phase synthesisspa
dc.subject.keywordMusspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordRodentiaspa
dc.subject.keywordAntibodieseng
dc.subject.keywordAntigen-antibody reactionsspa
dc.subject.keywordAntigenseng
dc.subject.keywordComputational biologyspa
dc.subject.keywordEpitopesspa
dc.subject.keywordMalaria vaccinesspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordProtozoan proteinsspa
dc.subject.keywordAntibodyspa
dc.subject.keywordMalaria vaccine candidatespa
dc.subject.keywordPassive immunizationspa
dc.subject.keywordPeptide mimeticspa
dc.subject.keywordPeptide-bond isosterespa
dc.subject.keywordSite-directed designspa
dc.titleRedefining an epitope of a malaria vaccine candidate, with antibodies against the N-terminal MSA-2 antigen of Plasmodium harboring non-natural peptide bondsspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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