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Monitoring Activation of the Antiviral Pattern Recognition Receptors RIG-I And PKR By Limited Protease Digestion and Native PAGE
Published on: July 29, 2014
El sensor viral citosólico RIG-I es una translocación dependiente de 5'-trifosfato en el ARN de doble cadena
Sua Myong1, Sheng Cui, Peter V Cornish
1Institute for Genomic Biology, University of Illinois at Urbana-Champaign, 1206 West Gregory Drive, Champaign, IL 61801, USA. smyong@uiuc.edu
Science (New York, N.Y.)
|January 3, 2009
Resumen
El gen inducible al ácido retinoico I (RIG-I) utiliza 5'-trifosfato para impulsar su movimiento a lo largo del ARN de doble cadena (dsRNA). Este mecanismo ayuda a RIG-I a distinguir el ARN viral del propio ARN, mejorando la inmunidad antiviral.
Área de la Ciencia:
- Inmunología Inmunología.
- Biología Molecular Biología Molecular
- Virología Virología.
Sus antecedentes:
- El gen inducible al ácido retinoico I (RIG-I) es un sensor citosólico clave del ARN viral, que inicia las respuestas inmunes antivirales.
- La señalización de RIG-I se basa en sus dominios de activación y reclutamiento de la caspasa N-terminal (CARD) y un dominio regulador, que discrimina entre el ARN patógeno y el propio ARN utilizando motivos de 5'-trifosfato y ARN de doble cadena (dsRNA).
- El papel preciso del dominio de helicasa de la caja DExH en la función de RIG-I seguía siendo menos entendido.
Objetivo del estudio:
- Para aclarar la función del dominio de helicasa de la caja DExH en RIG-I.
- Investigar el mecanismo por el cual RIG-I discrimina entre el ARN viral y el propio.
- Comprender el papel de las estructuras de ATP y ARN en la activación y translocación de RIG-I.
Principales métodos:
- Se empleó la mejora de fluorescencia inducida por proteínas de una sola molécula (smPIFE) para observar la actividad de RIG-I a nivel de una sola molécula.
- El estudio analizó la translocación de RIG-I en dsRNA en presencia y ausencia de 5'-trifosfato.
Principales resultados:
- RIG-I exhibe una robusta actividad de translocación impulsada por adenosina 5'-trifosfato en el dsRNA.
- Las CARD de RIG-I suprimen significativamente la translocación del dsRNA sin el 5'-trifosfato.
- La activación por 5'-trifosfato permite a RIG-I translocarse preferentemente en dsRNA en cis, lo que indica un mecanismo de detección coordinado.
Conclusiones:
- Los hallazgos revelan una nueva función de translocación de dsRNA dependiente de ATP para RIG-I.
- La integración de la detección de 5'-trifosfato y dsRNA proporciona un mecanismo sofisticado para que RIG-I detecte y responda específicamente a los virus que se replican.
- Este estudio mejora nuestra comprensión de la detección inmune innata de los patógenos virales.
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