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In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation
Published on: March 27, 2016
Estructura del virus del dengue inmaduro en bajos valores de pH primos maduración proteolítica
I-Mei Yu1, Wei Zhang, Heather A Holdaway
1Department of Biological Sciences, 915 West State Street, Purdue University, West Lafayette, IN 47907-2054, USA.
Science (New York, N.Y.)
|March 29, 2008
Resumen
Los flavivirus inmaduros experimentan un cambio de conformación dependiente del pH, lo que permite la escisión por furin. Este proceso estabiliza el virus dentro de la vía secretora de la célula huésped, evitando la fusión prematura de la membrana.
Área de la Ciencia:
- Virología Virología.
- Biología Estructural Biología estructural.
- Biología celular Biología celular.
Sus antecedentes:
- La maduración del flavivirus implica la escisión intracelular de las partículas inmaduras.
- El potencial de fusión de la glicoproteína E se genera durante este paso de escisión.
- Comprender este proceso es clave para controlar la infección por flavivirus.
Objetivo del estudio:
- Para aclarar los cambios estructurales y el mecanismo de la escisión del flavivirus inmaduro.
- Para investigar el papel del pH en el procesamiento y la estabilidad viral.
- Para revelar cómo se estabilizan los flavivirus en la red trans-Golgi.
Principales métodos:
- Se utilizó la microscopía criolectrónica para visualizar partículas de dengue inmaduras.
- El análisis estructural se realizó en diferentes condiciones de pH.
- Se realizaron ensayos de disociación dependientes del pH.
Principales resultados:
- Los flavivirus inmaduros experimentan un cambio conformacional reversible a un pH bajo (6.0).
- Este cambio expone la glicoproteína E a la escisión de la furin, formando un patrón de hueso de arenque.
- La disociación del péptido pr es dependiente del pH, lo que impide la fusión en ambientes ácidos.
Conclusiones:
- Se propone un nuevo mecanismo para el procesamiento y la estabilización del flavivirus en la vía secretora.
- Un pH bajo en la red trans-Golgi retiene el péptido pr, inhibiendo la fusión prematura de la membrana.
- Este mecanismo de escisión y estabilización es crítico para el ensamblaje y la infectividad de los flavivirus.
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