Actividad de unión a reticulocitos humanos del fragmento conservado de la proteína PvMSP10

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dc.contributor.advisorMoreno Pérez, Darwin Andrés
dc.contributor.advisorPatarroyo Gutiérrez, Manuel Alfonso
dc.contributor.authorRicaurte Contreras, Laura Alejandra
dc.contributor.researchgroupBiología Molecular de virusspa
dc.date.accessioned2021-06-24T17:53:27Z
dc.date.available2021-06-24T17:53:27Z
dc.date.issued2020
dc.descriptionilustracionesspa
dc.description.abstractPlasmodium vivax es una de las especies que causa malaria en humanos con mayor importancia epidemiológica en el mundo dada su amplia distribución geográfica. Esta especie es difícil de propagar in vitro dada su preferencia por invadir reticulocitos humanos y por ende su estudio biológico es complicado. Durante la invasión de estos parásitos a sus células diana se presenta un contacto inicial mediado principalmente por moléculas de superficie las cuales establecen diferentes interacciones proteína-proteína. Sin embargo, en P. vivax únicamente se conocen dos proteínas de superficie de merozoitos relacionadas con la adhesión específica a los reticulocitos humanos: MSP1 y RBSA. Dada la importancia de saber qué otras proteínas del parásito participan en el contacto inicial con el hospedero, en este estudio se evaluó, por primera vez, la capacidad de unión de la proteína de superficie de merozoito 10 (PvMSP10) a reticulocitos de humanos adultos. De particular interés, se encontró que PvMSP10 se une a reticulocitos humanos a través de la región C-terminal, cuyo polimorfismo es muy bajo. Además, mediante un ensayo de competición proteína-célula, se determinó que dicha interacción se encuentra gobernada por dos regiones de 20 residuos de longitud (388DKEECRCRANYMPDDSVDYF407 y 415KDCSKENGNCDVNAECSIDK434), que hacen parte de los dominios similares a EGF de esta proteína. Estos hallazgos destacan la importancia de dichos fragmentos para estudiar su utilidad en una futura vacuna contra la malaria causada por P. vivax. (Texto tomado de la fuente)spa
dc.description.abstractPlasmodium vivax is one of the species that causes malaria in humans with the greatest epidemiological importance in the world given its wide geographical distribution. This species is difficult to propagate in vitro given its preference for invading human reticulocytes and therefore its biological study is complicated. During the invasion of these parasites to their target cells, an initial contact occurs mainly mediated by surface molecules which establish different protein-protein interactions. However, only two merozoite surface proteins related to specific adhesion to human reticulocytes are known in P. vivax: MSP1 and RBSA. Given the importance of knowing which other parasite proteins are involved in the initial contact with the host, this study evaluated for the first time, the binding activity of merozoite surface protein 10 (PvMSP10) to adult human reticulocytes. It was found that PvMSP10 binds to human reticulocytes through the C-terminal region, whose polymorphism is low. Furthermore, by a protein-cell competition assay, it was determined that such interaction is governed by two regions of 20 residues in length (388DKEECRCRANYMPDDSVDYF407 and 415KDCSKENGNCDVNAECSIDK434), which are part of the EGF-like domains. These findings highlight the importance of these fragments to study their usefulness in a future vaccine against malaria caused by P. vivax. (Texto tomado de la fuente)eng
dc.description.degreelevelMaestríaspa
dc.description.degreenameMagíster en Ciencias - Microbiologíaspa
dc.description.researchareaBiología Molecular de Agentes Infecciososspa
dc.format.extent82 páginasspa
dc.format.mimetypeapplication/pdfspa
dc.identifier.instnameUniversidad Nacional de Colombiaspa
dc.identifier.reponameRepositorio Institucional Universidad Nacional de Colombiaspa
dc.identifier.repourlhttps://repositorio.unal.edu.co/spa
dc.identifier.urihttps://repositorio.unal.edu.co/handle/unal/79710
dc.language.isospaspa
dc.publisherUniversidad Nacional de Colombiaspa
dc.publisher.branchUniversidad Nacional de Colombia - Sede Bogotáspa
dc.publisher.departmentInstituto de Biotecnología (IBUN)spa
dc.publisher.facultyFacultad de Cienciasspa
dc.publisher.placeBogotá, Colombiaspa
dc.publisher.programBogotá - Ciencias - Maestría en Ciencias - Microbiologíaspa
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dc.rightsDerechos Reservados al Autor, 2020spa
dc.rights.accessrightsinfo:eu-repo/semantics/openAccessspa
dc.rights.licenseAtribución-NoComercial-SinDerivadas 4.0 Internacionalspa
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/spa
dc.subject.ddc500 - Ciencias naturales y matemáticas::507 - Educación, investigación, temas relacionadosspa
dc.subject.decsInmunología
dc.subject.decsImmunology
dc.subject.decsPlasmodium vivax
dc.subject.decsMalaria
dc.subject.proposalPlasmodium vivaxspa
dc.subject.proposalInvasiónspa
dc.subject.proposalInteracciones proteína-proteínaspa
dc.subject.proposalPvMSP10spa
dc.subject.proposalReticulocitos humanosspa
dc.subject.proposalPlasmodium vivaxeng
dc.subject.proposalInvasioneng
dc.subject.proposalProtein-protein interactionseng
dc.subject.proposalPvMSP10eng
dc.subject.proposalHuman reticulocyteseng
dc.titleActividad de unión a reticulocitos humanos del fragmento conservado de la proteína PvMSP10spa
dc.title.translatedReticulocyte binding activity humans from the preserved fragment of the PvMSP10 proteineng
dc.typeTrabajo de grado - Maestríaspa
dc.type.coarhttp://purl.org/coar/resource_type/c_bdccspa
dc.type.coarversionhttp://purl.org/coar/version/c_ab4af688f83e57aaspa
dc.type.contentTextspa
dc.type.driverinfo:eu-repo/semantics/masterThesisspa
dc.type.redcolhttp://purl.org/redcol/resource_type/TMspa
dc.type.versioninfo:eu-repo/semantics/acceptedVersionspa
dcterms.audienceGeneralspa
oaire.accessrightshttp://purl.org/coar/access_right/c_abf2spa
oaire.fundernameFundación Instituto Inmunología de Colombiaspa

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