Microbial Pathogen-induced Necrotic Cell Death Mediated by the Inflammasome Components CIAS1/cryopyrin/NLRP3 and ASC

Overview

Journal Cell Host Microbe

Publisher Cell Press

Specialties Infectious Diseases
Microbiology

Date 2007 Nov 17

PMID 18005730

Citations 150

Authors

Stephen B Willingham

Daniel T Bergstralh

William OConnor

Amy C Morrison

Debra J Taxman

Joseph A Duncan

Shoshana Barnoy

Malabi M Venkatesan

Richard A Flavell

Mohanish Deshmukh

Hal M Hoffman

Jenny P-Y Ting

Affiliations

Soon will be listed here.

Abstract

Cryopyrin (CIAS1, NLRP3) and ASC are components of the inflammasome, a multiprotein complex required for caspase-1 activation and cytokine IL-1beta production. CIAS1 mutations underlie autoinflammation characterized by excessive IL-1beta secretion. Disease-associated cryopyrin also causes a program of necrosis-like cell death in macrophages, the mechanistic details of which are unknown. We find that patient monocytes carrying disease-associated CIAS1 mutations exhibit excessive necrosis-like death by a process dependent on ASC and cathepsin B, resulting in spillage of the proinflammatory mediator HMGB1. Shigella flexneri infection also causes cryopyrin-dependent macrophage necrosis with features similar to the death caused by mutant CIAS1. This necrotic death is independent of caspase-1 and IL-1beta, and thus independent of the inflammasome. Furthermore, necrosis of primary macrophages requires the presence of Shigella virulence genes. While similar proteins mediate pathogen-induced cell death in plants, this report identifies cryopyrin as an important host regulator of programmed pathogen-induced necrosis in animals, a process we term pyronecrosis.

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