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El enjaulado NLRP3 domestica la actividad inflamatoria

Kate Schroder¹, Rebecca C Coll²

¹Institute for Molecular Bioscience and IMB Centre for Inflammation and Disease Research, The University of Queensland, St. Lucia, QLD 4072, Australia.

|December 23, 2021

Resumen

El inflamatorio NLRP3, un sensor de peligro clave, está regulado por una nueva estructura de doble anillo. Esta forma inactiva protege los dominios de pirina, revelando un nuevo mecanismo para el control del inflamatorio.

Área de la Ciencia:

Inmunología
Biología molecular
Biología estructural

Sus antecedentes:

El mecanismo de activación del inflamatorio NLRP3, un componente crítico de la inmunidad innata, sigue siendo incompleto.
La activación del NLRP3 está implicada en varias enfermedades inflamatorias.

Objetivo del estudio:

Para aclarar la base estructural del inflamatorio NLRP3 inactivo.
Descubrir el mecanismo que regula la activación del inflamatorio NLRP3.

Principales métodos:

Se utilizó la criomicroscopia electrónica (crio-EM) para determinar la estructura del NLRP3 inactivo.
Se realizaron análisis bioquímicos y estructurales.

Principales resultados:

NLRP3 inactivo forma un doble anillo estable compuesto de 12 a 16 monómeros.
Esta estructura de doble anillo secuestra los dominios de pirina, impidiendo el ensamblaje espontáneo del inflamasoma.
Cryo-EM reveló la arquitectura precisa del complejo inactivo.

Conclusiones:

La activación del inflamatorio NLRP3 está regulada por un mecanismo inhibidor de doble anillo no reconocido anteriormente.
Este descubrimiento proporciona nuevos conocimientos sobre el ensamblaje y la regulación del inflamatorio.
Los hallazgos ofrecen objetivos potenciales para la intervención terapéutica en condiciones inflamatorias asociadas con NLRP3.

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