Ítem
Solo Metadatos

Immunogenicity and protectivity of Plasmodium falciparum EBA-175 peptide and its analog is associated with alpha-helical region shortening and displacement

Mostrar el registro sencillo de la publicación
dc.creatorBermúdez, A.spa
dc.creatorCifuentes, G.spa
dc.creatorGuzmán, F.spa
dc.creatorSalazar, L. M.spa
dc.creatorPatarroyo, M. E.spa
dc.date.accessioned2020-08-19T14:44:13Z
dc.date.available2020-08-19T14:44:13Z
dc.date.created2003spa
dc.description.abstractEBA-175 protein is used as a ligand in the binding of P. falciparum to red blood cells (RBCs). Evidence shows that the conserved peptide 1779 from this protein (with high red blood cell binding ability and known critical erythrocyte binding residues) plays an important role in the invasion process. This peptide is neither immunogenic nor protective; analogs having critical residues replaced by amino acids with similar volume or mass but different polarity were synthesized and inoculated into Aotus monkeys, and elicited different immunogenic and protective responses. Nuclear Magnetic Resonance (1H-NMR) studies revealed that peptide analog 21696 (non-immunogenic and non-protective) presents a large helical fragment, that the peptide 14012 (immunogenic and non-protective) helical fragment is smaller, while the peptide 22812 (immunogenic and protective) [alpha]-helix is shorter in a different region and possesses greater flexibility at its N-terminus. The presence of methionine residues could affect the structural stability of peptide 22812 and ultimately its immunological response. Our results suggest a new strategy for designing a new malaria multi-component subunit-based vaccine.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1515/BC.2003.160
dc.identifier.issnISSN: 1431-6730
dc.identifier.issnEISSN: 1437-4315
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/27847
dc.language.isoengspa
dc.publisherWalter de Gruyterspa
dc.relation.citationEndPage1450
dc.relation.citationIssueNo. 10-11
dc.relation.citationStartPage1443
dc.relation.citationTitleBiological Chemistry
dc.relation.citationVolumeVol. 384
dc.relation.ispartofBiological Chemistry, ISSN: 1431-6730;EISSN: 1437-4315, Vol.384, No.10-11 (Oct.-Nov. 2003); pp. 1443-1450 spa
dc.relation.urihttps://www.degruyter.com/view/journals/bchm/384/10-11/article-p1443.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.keywordImmune responsespa
dc.subject.keywordMalariaspa
dc.subject.keywordNMRspa
dc.subject.keywordStructurespa
dc.titleImmunogenicity and protectivity of Plasmodium falciparum EBA-175 peptide and its analog is associated with alpha-helical region shortening and displacementspa
dc.title.TranslatedTitleLa inmunogenicidad y la capacidad de protección del péptido Plasmodium falciparum EBA-175 y su análogo se asocian con el acortamiento y el desplazamiento de la región alfa-helicoidalspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
Archivos
Colecciones
Artículos