التفاصيل البيبلوغرافية
العنوان: |
Identification of a cytoplasmic tryparedoxin peroxidase from Leishmania braziliensis ; Identificación de una triparedoxina peroxidasa citoplasmática en Leishmania braziliensis ; Identificação de uma triparedoxina peroxidase citoplasmica de Leishmania braziliensis |
المؤلفون: |
Villamil-Silva, Sharon Eliana, Ortiz-Joya, Lesly Johanna, Contreras-Rodríguez, Luis Ernesto, Díaz- Gonzalez, Gonzalo Jair, Ramírez-Hernández, María Helena |
المصدر: |
Revista Colombiana de Química; 2021: Vol. 50 Núm. 2; 3-14 ; 2357-3791 ; 0120-2804 |
بيانات النشر: |
Universidad Nacional de Colombia - Sede Bogotá - Facultad de Ciencias - Departamento de Química |
سنة النشر: |
2021 |
المجموعة: |
Universidad Nacional de Colombia: Portal de Revistas UN |
مصطلحات موضوعية: |
Anticuerpos policlonales IgY, Interacción proteína-proteína, Leishmania braziliensis, Localización celular, Tryparedoxin peroxidasa, Anticorpos policlonais IgY, Interação proteína-proteína, localização celular, Triparedoxina peroxidase, IgY polyclonal antibodies, Protein-protein interaction, Subcellular localization, Tryparedoxin peroxidase |
الوصف: |
The antioxidant defense systems used by the intracellular parasite Leishmania braziliensis during the infection process make it possible to eliminate reactive oxygen and nitrogen species at the expense of reducing equivalents derived from trypanothione, avoiding cellular damage of the pathogen. In order to identify potential molecular targets for the development of drugs against this parasite, the cytoplasmic tryparedoxin peroxidase of L. braziliensis (LbTXNPxII), which is essential to reduce toxic concentrations of hydrogen peroxide in the context of infection, was carried out. In this regard, polyclonal antibodies were generated in an avian model, starting from the cloning, expression, and purification of the recombinant protein 6xHis-SUMO-LbTXNPxII (37kDa) in the heterologous system of Escherichia coli. The purified protein was used as an antigen for the production of IgY antibodies, whose implementation in in situ experiments allowed the detection and localization of the endogenous LbTXNPxII enzyme (22kDa) in the cytoplasm of fixed promastigotes, as well as the verification of its molecular interaction with nicotinamide/nicotinate mononucleotide adenylyltransferase, an enzyme involved in the synthesis of NAD. Thus, the development of a biochemical tool for the identification and study of the LbTXNPxII enzyme and its participation in energy metabolism and antioxidant defense pathways is reported. ; Los sistemas de defensa anti-oxidante utilizados por el parásito intracelular Leishmania braziliensis durante el proceso de infección permiten eliminar especies reactivas de oxígeno y nitrógeno a expensas de equivalentes reductores derivados de la tripanotiona, evitando daños celulares del patógeno. Con el objetivo de identificar potenciales blancos moleculares para el desarrollo de fármacos contra este parásito, se realizó la detección de la enzima triparedoxina peroxidasa citoplasmática de L. braziliensis (LbTXNPxII), la cual es esencial para disminuir concentraciones tóxicas de peróxido de hidrógeno en el ... |
نوع الوثيقة: |
article in journal/newspaper |
وصف الملف: |
text/html; text/xml; application/pdf |
اللغة: |
Spanish; Castilian |
Relation: |
https://revistas.unal.edu.co/index.php/rcolquim/article/view/91721/81500; https://revistas.unal.edu.co/index.php/rcolquim/article/view/91721/81501; https://revistas.unal.edu.co/index.php/rcolquim/article/view/91721/80888; https://revistas.unal.edu.co/index.php/rcolquim/article/view/91721 |
الاتاحة: |
https://revistas.unal.edu.co/index.php/rcolquim/article/view/91721 |
Rights: |
Derechos de autor 2021 Sharon Eliana Villamil-Silva, Lesly Johanna Ortiz-Joya, Luis Ernesto Contreras-Rodríguez, Gonzalo Jair Díaz- Gonzalez & María Helena Ramírez-Hernández ; https://creativecommons.org/licenses/by/4.0 |
رقم الانضمام: |
edsbas.B69E8B40 |
قاعدة البيانات: |
BASE |