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Plasmodium falciparum TryThrA antigen synthetic peptides block in vitro merozoite invasion to erythrocytes

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dc.creatorCurtidor, Hernandospa
dc.creatorOcampo, Marisol
dc.creatorRodríguez, Luis E.spa
dc.creatorLópez, Ramsesspa
dc.creatorGarc??a, Javier E.spa
dc.creatorValbuena, Johnspa
dc.creatorVera, Ricardospa
dc.creatorPuentes, Álvarospa
dc.creatorLeiton, Jesusspa
dc.creatorCortes, Lina J.spa
dc.creatorLópez, Yolandaspa
dc.creatorPatarroyo, Manuel A.spa
dc.creatorPatarroyo, Manuel E.spa
dc.date.accessioned2020-08-06T16:20:22Z
dc.date.available2020-08-06T16:20:22Z
dc.date.created2006-01-20spa
dc.description.abstractTryptophan–threonine-rich antigen (TryThrA) is a Plasmodium falciparum homologue of Plasmodium yoelii-infected erythrocyte membrane pypAg-1 antigen. pypAg-1 binds to the surface of uninfected mouse erythrocytes and has been used successfully in vaccine studies. The two antigens are characterized by an unusual tryptophan-rich domain, suggesting similar biological properties. Using synthetic peptides spanning the TryThrA sequence and human erythrocyte we have done binding assays to identify possible TryThrA functional regions. We describe four peptides outside the tryptophan-rich domain having high activity binding to normal human erythrocytes. The peptides termed HABPs (high activity binding peptides) are 30884 (61LKEKKKKVLEFFENLVLNKKY80) located at the N-terminal and 30901 (401RKSLEQQFGDNMDKMNKLKKY420), 30902 (421KKILKFFPLFNYKSDLESIM440) and 30913 (641DLESTAEQKAEKKGGKAKAKY660) located at the C-terminal. Studies with polyclonal goat antiserum against synthetic peptides chosen to represent the whole length of the protein showed that TryThrA has fluorescence pattern similar to PypAg-1 of P. yoelii. All HABPs inhibited merozoite in vitro invasion, suggesting that TryThrA protein may be participating in merozoite–erythrocyte interaction during invasion.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1016/j.bbrc.2005.11.089
dc.identifier.issnISSN: 0006-291X
dc.identifier.issnEISSN: 1090-2104
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/25978
dc.language.isoengspa
dc.publisherElsevierspa
dc.relation.citationEndPage896
dc.relation.citationIssueNo. 3
dc.relation.citationStartPage888
dc.relation.citationTitleBiochemical and Biophysical Research Communications
dc.relation.citationVolumeVol. 339
dc.relation.ispartofBiochemical and Biophysical Research Communications, ISSN: 0006-291X;EISSN: 1090-2104, Vol.339, No.3 (2006); pp.888-896spa
dc.relation.urihttps://www.sciencedirect.com/science/article/abs/pii/S0006291X05026240spa
dc.rights.accesRightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.accesoRestringido (Acceso a grupos específicos)spa
dc.sourceBiochemical and Biophysical Research Communicationsspa
dc.source.instnameinstname:Universidad del Rosario
dc.source.reponamereponame:Repositorio Institucional EdocUR
dc.subject.keywordPeptidesspa
dc.subject.keywordTryptophan-threonine-rich antigenspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordMalariaspa
dc.subject.keywordInvasionspa
dc.titlePlasmodium falciparum TryThrA antigen synthetic peptides block in vitro merozoite invasion to erythrocytesspa
dc.title.TranslatedTitleLos péptidos sintéticos antígeno TryThrA de Plasmodium falciparum bloquean la invasión in vitro de merozoitos a los eritrocitosspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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