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Characterisation of Plasmodium falciparum RESA-like protein peptides that bind specifically to erythrocytes and inhibit invasion

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dc.creatorRodriguez, Luis Eduardospa
dc.creatorVera, Ricardospa
dc.creatorValbuena, Johnspa
dc.creatorCurtidor, Hernandospa
dc.creatorGarcia, Javierspa
dc.creatorPuentes, Alvarospa
dc.creatorOcampo, Marisol
dc.creatorLopez, Ramsesspa
dc.creatorRosas, Jaiverspa
dc.creatorLopez, Yolandaspa
dc.creatorPatarroyo, Manuel A.spa
dc.creatorPatarroyo, Manuel E.spa
dc.date.accessioned2020-08-19T14:41:51Z
dc.date.available2020-08-19T14:41:51Z
dc.date.created2007-01-10spa
dc.description.abstractThe Plasmodium falciparum ring-erythrocyte surface antigen (RESA)-like putative protein was identified and characterised. PCR and RT-PCR assays revealed that the gene encoding this protein was both present and being transcribed in P. falciparum strain FCB-2 16 h after erythrocyte invasion. Indirect immunofluorescence studies detected this protein in infected erythrocyte (IE) cytosol in dense fluorescent granules similar to Maurer's clefts at 16–20 h (parasites in ring and trophozoite stages) and very strongly on IE membranes at 22 h, suggesting that it is synthesised during early ring stages (16 h) and transported to the infected red blood cell (RBC) membrane surface during the trophozoite stage (22 h). Western blotting showed that antisera produced against polymerised synthetic peptides of this protein recognised a 72-kDa band in P. falciparum schizont lysate. P. falciparum RESA-like peptides used in normal RBC binding assays revealed that peptides 30326 (101NAEKI LGFDD KNILE ALDLFY120), 30334 (281RVTWK KLRTK MIKAL KKSLTY300) and 30342 (431SSPQR LKFTA GGGFC GKLRNY450) bind with high activity and saturability, presenting nM affinity constants. These peptides contain ?-helical structural elements, as determined by circular dichroism, and inhibit P. falciparum in vitro invasion of normal RBCs by up to 91%, suggesting that some RESA-like protein regions are involved in intra-erythrocyte stage P. falciparum invasion.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1515/BC.2007.002
dc.identifier.issnISSN: 1431-6730
dc.identifier.issnEISSN: 1437-4315
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/27352
dc.language.isoengspa
dc.publisherWalter de Gruyterspa
dc.relation.citationEndPage24
dc.relation.citationIssueNo. 1
dc.relation.citationStartPage15
dc.relation.citationTitleBiological Chemistry
dc.relation.citationVolumeVol. 388
dc.relation.ispartofBiological Chemistry, ISSN: 1431-6730 ; EISSN: 1437-4315, Vol.388, No.1 (Jan 2007); pp. 15-24 spa
dc.relation.urihttps://www.degruyter.com/view/journals/bchm/388/1/article-p15.xmlspa
dc.rights.accesRightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.accesoRestringido (Acceso a grupos específicos)spa
dc.sourceBiological Chemistryspa
dc.source.instnameinstname:Universidad del Rosario
dc.source.reponamereponame:Repositorio Institucional EdocUR
dc.subject.keywordBinding peptidespa
dc.subject.keywordErythrocytespa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordRESA-like proteinspa
dc.titleCharacterisation of Plasmodium falciparum RESA-like protein peptides that bind specifically to erythrocytes and inhibit invasionspa
dc.title.TranslatedTitleCaracterización de péptidos proteicos similares a RESA de Plasmodium falciparum que se unen específicamente a eritrocitos e inhiben la invasiónspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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