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Identifying Plasmodium falciparum cytoadherence-linked asexual protein 3 (CLAG 3) sequences that specifically bind to C32 cells and erythrocytes

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dc.creatorOcampo, Marisol
dc.creatorRodríguez, Luis E.spa
dc.creatorCurtidor, Hernandospa
dc.creatorPuentes, Álvarospa
dc.creatorVera, Ricardospa
dc.date.accessioned2020-08-19T14:44:10Z
dc.date.available2020-08-19T14:44:10Z
dc.date.created2005-02spa
dc.description.abstractAdhesion of mature asexual stage Plasmodium falciparum parasite-infected erythrocytes (iRBC) to thevascular endothelium is a critical event in the pathology of Plasmodium falciparum malaria. It has beensuggested that the clag gene family is essential in cytoadherence to endothelial receptors. Primers used inPCR and RT-PCR assays allowed us to determine that the gene encoding CLAG 3 (GenBank accession no.NP_473155) is transcribed in the Plasmodium falciparum FCB2 strain. Western blot showed that antiseraproduced against polymerized synthetic peptides from this protein recognized a 142-kDa band in P. falci-parum schizont lysate. Seventy-one 20-amino-acid-long nonoverlapping peptides, spanning the CLAG 3(cytoadherence-linked asexual protein on chromosome 3) sequence were tested in C32 cell and erythrocytebinding assays. Twelve CLAG peptides specifically bound to C32 cells (which mainly express CD36) withhigh affinity, hereafter referred to as high-affinity binding peptides (HABPs). Five of them also bound toerythrocytes. HABP binding to C32 cells and erythrocytes was independent of peptide charge or peptidestructure. Affinity constants were between 100 nM and 800 nM. Cross-linking and SDS-PAGE analysisallowed two erythrocyte binding proteins of around 26 kDa and 59 kDa to be identified, while proteins ofaround 53 kDa were identified as possible receptor sites for C-32 cells. The HABPs’ role in Plasmodiumfalciparum invasion inhibition was determined. Such an approach analyzing various CLAG 3 regions mayelucidate their functions and may help in the search for new antigens important for developing antimalarialvaccines.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1110/ps.04883905
dc.identifier.issnISSN: 0961-8368
dc.identifier.issnEISSN: 1469-896X
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/27840
dc.language.isoengspa
dc.publisherThe Protein Societyspa
dc.publisherJohn Wiley & Sonspa
dc.relation.citationEndPage513
dc.relation.citationIssueNo. 2
dc.relation.citationStartPage504
dc.relation.citationTitleProtein Science
dc.relation.citationVolumeVol. 14
dc.relation.ispartofProtein Science, ISSN: 0961-8368;EISSN: 1469-896X, Vol.14, No.2 (February 2005); pp. 504-513spa
dc.relation.urihttps://onlinelibrary.wiley.com/doi/epdf/10.1110/ps.04883905spa
dc.rights.accesRightsinfo:eu-repo/semantics/openAccess
dc.rights.accesoAbierto (Texto Completo)spa
dc.sourceProtein Sciencespa
dc.source.instnameinstname:Universidad del Rosario
dc.source.reponamereponame:Repositorio Institucional EdocUR
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordCytoadherencespa
dc.subject.keywordC32 cellsspa
dc.subject.keywordPeptidesspa
dc.subject.keywordCLAGspa
dc.subject.keywordcytoadherence?linked asexual proteinspa
dc.subject.keywordHABPsspa
dc.subject.keywordhigh activity binding peptidesspa
dc.subject.keywordPRBCsspa
dc.subject.keywordparasitized red blood cells HBSspa
dc.subject.keywordHEPES buffered salinespa
dc.titleIdentifying Plasmodium falciparum cytoadherence-linked asexual protein 3 (CLAG 3) sequences that specifically bind to C32 cells and erythrocytesspa
dc.title.TranslatedTitleIdentificación de secuencias de la proteína asexual 3 unida por citoadherencia de Plasmodium falciparum (CLAG 3) que se unen específicamente a células C32 y eritrocitosspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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