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Synthetic peptides from two Pf sporozoite invasion-associated proteins specifically interact with HeLa and HepG2 cells

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dc.creatorArévalo-Pinzón G.spa
dc.creatorCurtidor H.spa
dc.creatorMuñoz M.spa
dc.creatorPatarroyo M.A.spa
dc.creatorPatarroyo M.E.spa
dc.date.accessioned2020-05-25T23:58:02Z
dc.date.available2020-05-25T23:58:02Z
dc.date.created2011spa
dc.description.abstractTwo recently described molecules have been associated with sporozoite traversal ability and hepatocyte entry: sporozoite invasion-associated proteins (SIAP)-1 and -2. The HeLa and HepG2 cell binding ability of synthetic peptides spanning the whole SIAP-1 and -2 sequences has been studied in the search for identifying these proteins' functionally active specific regions. Twelve HepG-2 and seventeen HeLa cell high-activity binding peptides (HABPs) have been identified in SIAP-1, 8 of them having high specific binding affinity for both cell lines. Four HepG2 HABPs and two HeLa HABPs have been identified in SIAP-2, one of them interacting with both HeLa and HepG2 cells. SIAP-1 and SIAP-2 HABPs bound specifically and saturably to heparin sulfate and chondroitin sulfate-type membrane receptors on host cells. Circular dichroism assays have shown high ?-helix content in SIAP-1 and SIAP-2 HABP secondary structure. Immunofluorescence analysis has revealed that specific peptides against SIAP proteins are highly immunogenic in mice and that anti-SIAP-1 and -2 antibodies recognize the native protein in Plasmodium falciparum sporozoites. Polymorphism studies have shown that a most SIAP-1 and -2 HABPs are conserved among P. falciparum strains. Our results have suggested that SIAP-1 and -2 participate in host-pathogen interactions during cell-traversal and hepatocyte invasion and highlighted the relevance of the ongoing identification and study of potentially new molecules when designing a fully protective antimalarial vaccine. © 2011 Elsevier Inc.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1016/j.peptides.2011.08.008
dc.identifier.issn1969781
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/22791
dc.language.isoengspa
dc.relation.citationEndPage1908
dc.relation.citationIssueNo. 9
dc.relation.citationStartPage1902
dc.relation.citationTitlePeptides
dc.relation.citationVolumeVol. 32
dc.relation.ispartofPeptides, ISSN:1969781, Vol.32, No.9 (2011); pp. 1902-1908spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-80052696685&doi=10.1016%2fj.peptides.2011.08.008&partnerID=40&md5=453abc66ec5fd0d4ecf9a6dec95bc2afspa
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.keywordChondroitin sulfatespa
dc.subject.keywordgeneticeng
dc.subject.keywordHeparinspa
dc.subject.keywordProtein siap 1spa
dc.subject.keywordProtein siap 2spa
dc.subject.keywordUnclassified drugspa
dc.subject.keywordArticlespa
dc.subject.keywordBinding affinityspa
dc.subject.keywordCircular dichroismspa
dc.subject.keywordControlled studyspa
dc.subject.keywordGenetic polymorphismspa
dc.subject.keywordHumanspa
dc.subject.keywordHuman cellspa
dc.subject.keywordImmunofluorescence testspa
dc.subject.keywordImmunogenicityspa
dc.subject.keywordLiver cellspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordPriority journalspa
dc.subject.keywordProtein analysisspa
dc.subject.keywordProtein interactionspa
dc.subject.keywordProtein synthesisspa
dc.subject.keywordSporozoitespa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordAnimalsspa
dc.subject.keywordBinding sitesspa
dc.subject.keywordChemistry techniqueseng
dc.subject.keywordChondroitin sulfatesspa
dc.subject.keywordCircular dichroismspa
dc.subject.keywordFluorescent antibody techniqueeng
dc.subject.keywordHela cellsspa
dc.subject.keywordHep g2 cellsspa
dc.subject.keywordHepatocytesspa
dc.subject.keywordHost-pathogen interactionsspa
dc.subject.keywordHumansspa
dc.subject.keywordMicespa
dc.subject.keywordMiceeng
dc.subject.keywordMolecular sequence dataspa
dc.subject.keywordPeptidesspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordPolymorphismeng
dc.subject.keywordProtein bindingspa
dc.subject.keywordProtozoan proteinsspa
dc.subject.keywordSporozoitesspa
dc.subject.keywordMusspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordAntimalarial vaccinespa
dc.subject.keywordCell-traversalspa
dc.subject.keywordHigh-activity binding peptidespa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordSporozoite invasionspa
dc.titleSynthetic peptides from two Pf sporozoite invasion-associated proteins specifically interact with HeLa and HepG2 cellsspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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