Division of Infectious Diseases and Immunology, Department of Medicine, UMass Medical School, Worcester, MA 01605, USA.
Curr Opin Microbiol. 2013 Feb;16(1):23-31. doi: 10.1016/j.mib.2012.11.008. Epub 2013 Jan 11.
The inflammasome has emerged as an important molecular protein complex which initiates proteolytic processing of pro-IL-1β and pro-IL-18 into mature inflammatory cytokines. In addition, inflammasomes initiate pyroptotic cell death that may be independent of those cytokines. Inflammasomes are central to elicit innate immune responses against many pathogens, and are key components in the induction of host defenses following bacterial infection. Here, we review recent discoveries related to NLRP1, NLRP3, NLRC4, NLRP6, NLRP7, NLRP12 and AIM2-mediated recognition of bacteria. Mechanisms for inflammasome activation and regulation are now suggested to involve kinases such as PKR and PKCδ, ligand binding proteins such as the NAIPs, and caspase-11 and caspase-8 in addition to caspase-1. Future research will determine how specific inflammasome components pair up in optimal responses to specific bacteria.
炎症小体已成为一种重要的分子蛋白复合物，可启动 pro-IL-1β 和 pro-IL-18 向成熟炎症细胞因子的蛋白水解加工。此外，炎症小体还启动可能独立于这些细胞因子的细胞焦亡。炎症小体是引发针对多种病原体固有免疫反应的核心，也是细菌感染后诱导宿主防御的关键组成部分。在这里，我们综述了与 NLRP1、NLRP3、NLRC4、NLRP6、NLRP7、NLRP12 和 AIM2 介导的细菌识别相关的最新发现。目前认为，炎症小体的激活和调节机制涉及蛋白激酶如 PKR 和 PKCδ、配体结合蛋白如 NAIPs，以及除 caspase-1 之外的 caspase-11 和 caspase-8。未来的研究将确定特定炎症小体成分如何与特定细菌的最佳反应相匹配。
