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Microbial pathogen-induced necrotic cell death mediated by the inflammasome components CIAS1/cryopyrin/NLRP3 and ASC.

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.

journal_name

Cell Host Microbe

journal_title

Cell host & microbe

authors

Willingham SB,Bergstralh DT,O'Connor W,Morrison AC,Taxman DJ,Duncan JA,Barnoy S,Venkatesan MM,Flavell RA,Deshmukh M,Hoffman HM,Ting JP

doi

10.1016/j.chom.2007.07.009

subject

Has Abstract

pub_date

2007-09-13 00:00:00

pages

147-59

issue

3

eissn

1931-3128

issn

1934-6069

pii

S1931-3128(07)00192-8

journal_volume

2

pub_type

杂志文章

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