Caracterización del complejo mayor de histocompatibilidad clase II en primates del género Aotus

El presente trabajo tiene como propósito contribuir al conocimiento del complejo mayor de histocompatibilidad clase II (CMH-II) de los monos Aotus, contribuyendo a la validación de este primate como modelo experimental, y aumentando el conocimiento en la evolución de los genes del CMH en primates. A...

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Fecha de publicación:
2017
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
spa
OAI Identifier:
oai:repository.urosario.edu.co:10336/13809
Acceso en línea:
https://doi.org/10.48713/10336_13809
http://repository.urosario.edu.co/handle/10336/13809
Palabra clave:
Complejo mayor de histocompatibilidad
Evolución molecular
Monos del nuevo mundo
Platyrrhini
Microsatélite D6S2878
Convergencia molecular
Estructura secundaria de proteínas
Sustituciones de aminoácidos
Matrices de mutación
Primates
PM7
FMO-PIEDA
DFTB
Interacción proteína-proteína
Unión CMH-péptido
Biología
Inmunología
Histocompatibilidad
Polimorfismo genético
Major histocompatibility complex
Molecular evolution
New world monkeys
Platyrrhini
D6S2878 microsatellite
Molecular convergence
MHC-peptide binding
Protein secondary structure
Substitution matrices
Primates
PM7
DFTB
FMO-PIEDA
protein-protein interaction
Inmunología
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License
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id EDOCUR2_7d90631022ea117bff088ed327dd94ea
oai_identifier_str oai:repository.urosario.edu.co:10336/13809
network_acronym_str EDOCUR2
network_name_str Repositorio EdocUR - U. Rosario
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dc.title.spa.fl_str_mv Caracterización del complejo mayor de histocompatibilidad clase II en primates del género Aotus
title Caracterización del complejo mayor de histocompatibilidad clase II en primates del género Aotus
spellingShingle Caracterización del complejo mayor de histocompatibilidad clase II en primates del género Aotus
Complejo mayor de histocompatibilidad
Evolución molecular
Monos del nuevo mundo
Platyrrhini
Microsatélite D6S2878
Convergencia molecular
Estructura secundaria de proteínas
Sustituciones de aminoácidos
Matrices de mutación
Primates
PM7
FMO-PIEDA
DFTB
Interacción proteína-proteína
Unión CMH-péptido
Biología
Inmunología
Histocompatibilidad
Polimorfismo genético
Major histocompatibility complex
Molecular evolution
New world monkeys
Platyrrhini
D6S2878 microsatellite
Molecular convergence
MHC-peptide binding
Protein secondary structure
Substitution matrices
Primates
PM7
DFTB
FMO-PIEDA
protein-protein interaction
Inmunología
title_short Caracterización del complejo mayor de histocompatibilidad clase II en primates del género Aotus
title_full Caracterización del complejo mayor de histocompatibilidad clase II en primates del género Aotus
title_fullStr Caracterización del complejo mayor de histocompatibilidad clase II en primates del género Aotus
title_full_unstemmed Caracterización del complejo mayor de histocompatibilidad clase II en primates del género Aotus
title_sort Caracterización del complejo mayor de histocompatibilidad clase II en primates del género Aotus
dc.contributor.advisor.none.fl_str_mv Cadavid Gutiérrez, Luis Fernando
Patarroyo, Manuel A.
dc.subject.spa.fl_str_mv Complejo mayor de histocompatibilidad
Evolución molecular
Monos del nuevo mundo
Platyrrhini
Microsatélite D6S2878
Convergencia molecular
Estructura secundaria de proteínas
Sustituciones de aminoácidos
Matrices de mutación
Primates
PM7
FMO-PIEDA
DFTB
Interacción proteína-proteína
Unión CMH-péptido
topic Complejo mayor de histocompatibilidad
Evolución molecular
Monos del nuevo mundo
Platyrrhini
Microsatélite D6S2878
Convergencia molecular
Estructura secundaria de proteínas
Sustituciones de aminoácidos
Matrices de mutación
Primates
PM7
FMO-PIEDA
DFTB
Interacción proteína-proteína
Unión CMH-péptido
Biología
Inmunología
Histocompatibilidad
Polimorfismo genético
Major histocompatibility complex
Molecular evolution
New world monkeys
Platyrrhini
D6S2878 microsatellite
Molecular convergence
MHC-peptide binding
Protein secondary structure
Substitution matrices
Primates
PM7
DFTB
FMO-PIEDA
protein-protein interaction
Inmunología
dc.subject.ddc.none.fl_str_mv Biología
dc.subject.decs.spa.fl_str_mv Inmunología
Histocompatibilidad
Polimorfismo genético
dc.subject.keyword.eng.fl_str_mv Major histocompatibility complex
Molecular evolution
New world monkeys
Platyrrhini
D6S2878 microsatellite
Molecular convergence
MHC-peptide binding
Protein secondary structure
Substitution matrices
Primates
PM7
DFTB
FMO-PIEDA
protein-protein interaction
dc.subject.lemb.spa.fl_str_mv Inmunología
description El presente trabajo tiene como propósito contribuir al conocimiento del complejo mayor de histocompatibilidad clase II (CMH-II) de los monos Aotus, contribuyendo a la validación de este primate como modelo experimental, y aumentando el conocimiento en la evolución de los genes del CMH en primates. Además, se profundizó en el análisis de convergencia y polimorfismo de los genes del CMH-DR en primates. Se implementaron metodologías de modelación computacional de la unión CMH-péptido, como herramientas necesarias para entender los mecanismos de presentación de péptidos por parte del CMH clase II a los linfocitos T. El estudio del polimorfismo de la región de unión al péptido, permitió el desarrollo de estrategias para reducir eficientemente el número de sistemas a considerar en el diseño de péptidos a ser usados como candidatos a vacuna contra la malaria. Usando minería de datos sobre distribuciones de Ramachandran, se desarrolló una escala de similitud estructural de aminoácidos, con el fin de implementar su uso en el desarrollo de péptidos candidatos a vacunas. Adicionalmente, se encontró que la estructura secundaria de las proteínas tiene una relación clara con los patrones evolutivos de sustitución y la mutabilidad de los aminoácidos. Así, se ha generado un marco de conceptual que contribuye al desarrollo de vacunas basadas en péptidos, que tiene como base el estudio del polimorfismo del complejo mayor de histocompatibilidad, las restricciones fisicoquímicas/estructurales que moldean el proceso de reconocimiento molecular involucrado en la interacción CMH-péptido y la aplicación de metodologías computacionales para cuantificar el proceso de unión CMH-péptido.
publishDate 2017
dc.date.accessioned.none.fl_str_mv 2017-10-11T13:59:03Z
dc.date.available.none.fl_str_mv 2017-10-11T13:59:03Z
dc.date.created.none.fl_str_mv 2017-10-05
dc.date.issued.none.fl_str_mv 2017
dc.type.eng.fl_str_mv doctoralThesis
dc.type.coar.fl_str_mv http://purl.org/coar/resource_type/c_db06
dc.type.spa.spa.fl_str_mv Tesis de doctorado
dc.identifier.doi.none.fl_str_mv https://doi.org/10.48713/10336_13809
dc.identifier.uri.none.fl_str_mv http://repository.urosario.edu.co/handle/10336/13809
url https://doi.org/10.48713/10336_13809
http://repository.urosario.edu.co/handle/10336/13809
dc.language.iso.none.fl_str_mv spa
language spa
dc.rights.coar.fl_str_mv http://purl.org/coar/access_right/c_abf2
dc.rights.acceso.spa.fl_str_mv Abierto (Texto completo)
rights_invalid_str_mv Abierto (Texto completo)
http://purl.org/coar/access_right/c_abf2
dc.format.mimetype.none.fl_str_mv application/pdf
dc.publisher.spa.fl_str_mv Universidad del Rosario
dc.publisher.department.spa.fl_str_mv Facultad de Ciencias Naturales y Matemáticas
dc.publisher.program.spa.fl_str_mv Doctorado en Ciencias Biomédicas
institution Universidad del Rosario
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spelling Cadavid Gutiérrez, Luis Fernandob0a4c91e-504d-4a43-b16b-80d4e9e84571-1Patarroyo, Manuel A.79653065600Suarez Martinez, Carlos FernandoDoctor en Ciencias Biomédicas796132306002017-10-11T13:59:03Z2017-10-11T13:59:03Z2017-10-052017El presente trabajo tiene como propósito contribuir al conocimiento del complejo mayor de histocompatibilidad clase II (CMH-II) de los monos Aotus, contribuyendo a la validación de este primate como modelo experimental, y aumentando el conocimiento en la evolución de los genes del CMH en primates. Además, se profundizó en el análisis de convergencia y polimorfismo de los genes del CMH-DR en primates. Se implementaron metodologías de modelación computacional de la unión CMH-péptido, como herramientas necesarias para entender los mecanismos de presentación de péptidos por parte del CMH clase II a los linfocitos T. El estudio del polimorfismo de la región de unión al péptido, permitió el desarrollo de estrategias para reducir eficientemente el número de sistemas a considerar en el diseño de péptidos a ser usados como candidatos a vacuna contra la malaria. Usando minería de datos sobre distribuciones de Ramachandran, se desarrolló una escala de similitud estructural de aminoácidos, con el fin de implementar su uso en el desarrollo de péptidos candidatos a vacunas. Adicionalmente, se encontró que la estructura secundaria de las proteínas tiene una relación clara con los patrones evolutivos de sustitución y la mutabilidad de los aminoácidos. Así, se ha generado un marco de conceptual que contribuye al desarrollo de vacunas basadas en péptidos, que tiene como base el estudio del polimorfismo del complejo mayor de histocompatibilidad, las restricciones fisicoquímicas/estructurales que moldean el proceso de reconocimiento molecular involucrado en la interacción CMH-péptido y la aplicación de metodologías computacionales para cuantificar el proceso de unión CMH-péptido.This work was aimed to contribute to increase our knowledge on the MHC class II in monkeys from the genus Aotus. Determining the sequences of MHC-DPA and MHC-DRA genes has allowed to complete the characterisation of the Aotus MHC, contributing towards validating the role of this primate as experimental model and increasing our knowledge regarding MHC gene evolution in primates. It also dealt with in–depth analysis of MHC-DR genes’ convergence and polymorphism in primates. The study involves computational modelling of MHC-peptide binding methodologies (based on quantum chemistry and neural networks) as necessary tools for understanding the mechanisms of MHC class II peptide presentation to T-lymphocytes. Studying peptide binding region polymorphism has enabled developing strategies (pocket profiles) for efficiently reducing the amount of systems to be considered when designing peptides to be used as candidates for an antimalarial vaccine. Data-mining regarding Ramachandran distribution led to developing an amino acid structural similarity scale for use in developing/designing peptides as vaccine candidates. It was found that protein secondary structure has a clear relationship with amino acid substitution and mutability evolutionary patterns. A conceptual framework thus emerged aimed at developing peptide-based vaccines as a basis for studying the mayor histocompatibility complex polymorphism, the physicochemical/structural restrictions shaping the molecular recognition involved in MHC-peptide interaction and using computational methodologies for quantifying MHC-peptide binding. application/pdfhttps://doi.org/10.48713/10336_13809 http://repository.urosario.edu.co/handle/10336/13809spaUniversidad del RosarioFacultad de Ciencias Naturales y MatemáticasDoctorado en Ciencias BiomédicasAbierto (Texto completo)EL AUTOR, manifiesta que la obra objeto de la presente autorización es original y la realizó sin violar o usurpar derechos de autor de terceros, por lo tanto la obra es de exclusiva autoría y tiene la titularidad sobre la misma. PARGRAFO: En caso de presentarse cualquier reclamación o acción por parte de un tercero en cuanto a los derechos de autor sobre la obra en cuestión, EL AUTOR, asumirá toda la responsabilidad, y saldrá en defensa de los derechos aquí autorizados; para todos los efectos la universidad actúa como un tercero de buena fe. EL AUTOR, autoriza a LA UNIVERSIDAD DEL ROSARIO, para que en los términos establecidos en la Ley 23 de 1982, Ley 44 de 1993, Decisión andina 351 de 1993, Decreto 460 de 1995 y demás normas generales sobre la materia, utilice y use la obra objeto de la presente autorización. -------------------------------------- POLITICA DE TRATAMIENTO DE DATOS PERSONALES. Declaro que autorizo previa y de forma informada el tratamiento de mis datos personales por parte de LA UNIVERSIDAD DEL ROSARIO para fines académicos y en aplicación de convenios con terceros o servicios conexos con actividades propias de la academia, con estricto cumplimiento de los principios de ley. 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