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Modelo tridimensional de las proteínas Nfcpb y Nfcpb-l de Naegleria Fowleri
dc.contributor.advisor | Posada Buitrago, Martha Lucia | |
dc.contributor.author | Castillo Vega, Leidy Gabriela | |
dc.date.accessioned | 2021-10-29T18:59:55Z | |
dc.date.available | 2021-10-29T18:59:55Z | |
dc.date.issued | 2019-01 | |
dc.identifier.uri | https://repositorio.unicolmayor.edu.co/handle/unicolmayor/3585 | |
dc.description.abstract | La meningoencefalitis amebiana primaria (PAM) es una enfermedad de amplia distribución a nivel mundial, con un porcentaje mayor de casos en climas tropicales. PAM es causada por una ameba de vida libre del genero Naegleria, de la cual han descrito 47 especies1, dos de estas especies son agentes causales de enfermedades en animales experimentales; mientras que solo una especie, Naegleria fowleri, es patógeno en los humanos. No existe un mecanismo de control para Naegleria fowleri, ya que se considera como una enfermedad poco frecuente. El análisis de proteínas actualmente se ha convertido en un principio fundamental para el estudio de posibles blancos terapéuticos que permitan la realización de vacunas que tengan un amplio rango de inmunización, y el conocimiento de las funciones de las proteínas. En el caso de Naegleria fowleri se han identificado factores de patogenicidad como las proteínas Catepsina B (NfCPB) y Catepsina B-L (NfCPB-L), primordiales en actividades proteolíticas sobre las Inmunoglobulinas, fibronectina, hemoglobina y albúmina, reconocimiento y anclaje celular.13 El objetivo de esta investigación fue proponer mediante el análisis bioinformático la estructura tridimensional de las proteínas NfCPB y NfCPB-L de Naegleria fowleri logrando así inferir las regiones funcionales asociadas importantes para su antigenicidad e inmunogenicidad. Para el análisis de la estructura primaria se determinaron las propiedades fisicoquímicas, el índice de hidrofobicidad y las regiones transmembranales. Para la estructura secundaria, se realizó un consenso 14 con seis algoritmos disponibles en el servidor NSP@. La aproximación de la estructura terciaria de la proteína se realizó por el programa I-TASSER y el modelamiento tridimensional se visualizó a través del servidor Swiss-Pdb Viewer 4.1.0, la validación del modelo se llevó a cabo por la gráfica de Ramachandran basándose en la distribución de ángulos de los aminoácidos que componen el modelo obtenido. Como resultado final de la investigación se obtuvieron dos modelos 3D consistentes, y una aproximación a la función de las proteínas NfCPB y NfCPB-L. | spa |
dc.description.tableofcontents | RESUMEN 11 1. INTRODUCCIÓN 13 2. OBJETIVOS 15 2.1. General 15 2.2. Específicos 15 3. ANTECEDENTES 16 4. MARCO DE REFERENCIA 18 4.1. Origen 18 4.2. Etiología y Morfología 18 4.3. Taxonomía 19 4.4. Transmisión 20 4.5. Patogenia 21 4.5.1. Mecanismos dependientes de contacto 22 4.5.2. Mecanismos independientes de contacto 23 4.6. Inmunología 24 4.6.1. Evasión Inmune 24 4.6.2. Inmunización 25 4.7. Meningoencefalitis amebiana primaria (PAM) 26 4.8. Epidemiología 27 8 4.9. Diagnóstico 28 4.10. Tratamiento 29 4.11. Proteínas NfCPB y NfCPB-L 29 4.12. Bioinformática 32 4.13. Predicción estructural de proteínas 33 4.13.1. Predicción de la estructura secundaria de proteínas 34 4.13.2. Predicción de la estructura terciaria de proteínas (I-TASSER) 34 5. DISEÑO METODOLÓGICO 36 5.1. Tipo de investigación 36 5.2. Hipótesis 36 6. TÉCNICAS Y PROCEDIMIENTOS 37 6.1. Herramientas para la búsqueda de similitud y homología de secuencias 37 6.2. Herramientas para el análisis de estructura primaria 37 6.3. Herramientas para el análisis de estructura secundaria 37 6.4. Herramientas para el análisis de estructura terciaria 38 7. RESULTADOS 40 7.1 Alineamiento de secuencias NfCPB y NfCPB-L de Naegleria fowleri con Clustal Omega 40 7.2. Análisis de la estructura primaria de NfCPB y NfCPB-L 41 7.3 Determinación de la estructura secundaria de las proteínas NfCPB y NfCPB-L de Naegleria fowleri 48 9 7.4 Determinación de la estructura tridimensional de las proteínas NfCPB y NfCPB-L de Naegleria fowleri 51 8. DISCUSIÓN 64 9. CONCLUSIONES 75 10. BIBLIOGRAFÍA 77 | spa |
dc.format.extent | 97p. | spa |
dc.format.mimetype | application/pdf | spa |
dc.language.iso | spa | spa |
dc.publisher | Universidad Colegio Mayor de Cundinamarca | spa |
dc.rights | Universidad Colegio Mayor de Cundinamarca, 2019 | spa |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-sa/4.0/ | spa |
dc.title | Modelo tridimensional de las proteínas Nfcpb y Nfcpb-l de Naegleria Fowleri | spa |
dc.type | Trabajo de grado - Pregrado | spa |
dc.description.degreelevel | Pregrado | spa |
dc.description.degreename | Bacteriólogo(a) y Laboratorista Clínico | spa |
dc.publisher.faculty | Facultad de Ciencias de la Salud | spa |
dc.publisher.place | Bogotá D.C | spa |
dc.publisher.program | Bacteriología y Laboratorio Clínico | spa |
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dc.relation.references | Debnath, A., Calvet, C. M., Jennings, G., Zhou, W., Aksenov, A., Luth, M. R., … Podust, L. M. (2017). CYP51 is an essential drug target for the | spa |
dc.rights.accessrights | info:eu-repo/semantics/closedAccess | spa |
dc.rights.creativecommons | Atribución-NoComercial-CompartirIgual 4.0 Internacional (CC BY-NC-SA 4.0) | spa |
dc.subject.lemb | Meningoencefalitis | |
dc.subject.lemb | Enfermedad | |
dc.subject.lemb | Especies | |
dc.subject.lemb | Animales experimentales | |
dc.subject.proposal | Bioinformática | spa |
dc.subject.proposal | Proteína | spa |
dc.subject.proposal | NfCPB | spa |
dc.subject.proposal | proteína NfCPB-L | spa |
dc.subject.proposal | Naegleria fowleri | spa |
dc.subject.proposal | Catepsina | spa |
dc.type.coar | http://purl.org/coar/resource_type/c_7a1f | spa |
dc.type.coarversion | http://purl.org/coar/version/c_970fb48d4fbd8a85 | spa |
dc.type.content | Text | spa |
dc.type.driver | info:eu-repo/semantics/bachelorThesis | spa |
dc.type.redcol | https://purl.org/redcol/resource_type/TP | spa |
dc.type.version | info:eu-repo/semantics/publishedVersion | spa |
dc.rights.coar | http://purl.org/coar/access_right/c_14cb | spa |