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Splenectomised and spleen intact Aotus monkeys' immune response to Plasmodium vivax MSP-1 protein fragments and their high activity binding peptides

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dc.creatorSierra, Adriana Yanettspa
dc.creatorBarrero, Carlos Albertospa
dc.creatorRodriguez, Raulspa
dc.creatorSilva, Yolandaspa
dc.creatorMoncada, Camilospa
dc.creatorVanegas, Magnoliaspa
dc.creatorPatarroyo, Manuel A.
dc.date.accessioned2020-08-28T15:47:55Z
dc.date.available2020-08-28T15:47:55Z
dc.date.created2003-10-01spa
dc.description.abstractTwo E. coli expressed recombinant polypeptides (rPvMSP-114 and rPvMSP-120) contained in the 33 kDa fragment, located within Plasmodium vivax merozoite surface protein (PvMSP-1) 42 kDa C-terminal region, and a cocktail of high reticulocyte binding synthetic peptides located within these fragments, were evaluated for immunogenicity and protective immune responses in splenectomised and spleen intact Aotus nancymaae monkeys. Thirty splenectomised monkeys who had been previously immunised with either rPvMSP-114, rPvMSP-120, or a mixture of both recombinant fragments were intravenously challenged with the heterologous P. vivax VCG-1 strain (as determined by DNA sequencing); full protection was observed in five monkeys and low parasitaemia levels were obtained in eight more monkeys. Splenectomised control monkey group rapidly developed high parasitaemia levels, while no significant parasitaemia was obtained in the non-splenectomised control group. Although PvMSP-1 42 and 33 kDa fragments were recognised by Western Blot and whole parasites by IFAT when tested with immune monkey sera, no correlation between protection and antibody titres by IFAT and ELISA was observed, suggesting that protection is not being solely mediated by a humoral immune response. This data showed that partial protection against a heterologous strain challenge was best achieved when immunising with a rPvMSP-114–rPvMSP-120 mixture (2 were fully protected and 4 with low parasitaemia out of 12) suggesting for the first time, that these fragments could be good candidates for inclusion in a P. vivax multi-stage, multi-antigen vaccine.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1016/S0264-410X(03)00455-9
dc.identifier.issnISSN: 0264-410X
dc.identifier.issnEISSN: 1873-2518
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/28305
dc.language.isoengspa
dc.publisherElsevierspa
dc.relation.citationEndPage4144
dc.relation.citationIssueNo. 27-30
dc.relation.citationStartPage4133
dc.relation.citationTitleVaccine
dc.relation.citationVolumeVol. 21
dc.relation.ispartofVaccine, ISSN: 0264-410X;EISSN: 1873-2518, Vol. 21, No. 27-30 (1 October 2003); pp. 4133-4144spa
dc.relation.urihttps://www.sciencedirect.com/science/article/pii/S0264410X03004559?via%3Dihubspa
dc.rights.accesRightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.accesoRestringido (Acceso a grupos específicos)spa
dc.sourceVaccinespa
dc.source.instnameinstname:Universidad del Rosario
dc.source.reponamereponame:Repositorio Institucional EdocUR
dc.subject.keywordPlasmodium vivaxspa
dc.subject.keywordMSP-1spa
dc.subject.keywordImmunisationspa
dc.subject.keyword33 kDa fragmentspa
dc.subject.keywordHeterologous challengespa
dc.titleSplenectomised and spleen intact Aotus monkeys' immune response to Plasmodium vivax MSP-1 protein fragments and their high activity binding peptidesspa
dc.title.TranslatedTitleRespuesta inmune de los monos Aotus esplenectomizados y con el bazo intacto a los fragmentos de proteína Plasmodium vivax MSP-1 y sus péptidos de unión de alta actividadspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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