Human NLRP3 Inflammasome senses multiple types of bacterial RNAs Academic Article uri icon

Overview

MeSH Major

  • Carrier Proteins
  • Inflammasomes
  • Macrophages
  • RNA, Bacterial
  • RNA, Messenger

abstract

  • Inflammasomes are multiprotein platforms that activate caspase-1, which leads to the processing and secretion of the proinflammatory cytokines IL-1β and IL-18. Previous studies demonstrated that bacterial RNAs activate the nucleotide-binding domain, leucine-rich-repeat-containing family, pyrin domain-containing 3 (NLRP3) inflammasome in both human and murine macrophages. Interestingly, only mRNA, but neither tRNA nor rRNAs, derived from bacteria could activate the murine Nlrp3 inflammasome. Here, we report that all three types of bacterially derived RNA (mRNA, tRNA, and rRNAs) were capable of activating the NLRP3 inflammasome in human macrophages. Bacterial RNA's 5'-end triphosphate moieties, secondary structure, and double-stranded structure were dispensable; small fragments of bacterial RNA were sufficient to activate the inflammasome. In addition, we also found that 20-guanosine ssRNA can activate the NLRP3 inflammasome in human macrophages but not in murine macrophages. Therefore, human and murine macrophages may have evolved to recognize bacterial cytosolic RNA differently during bacterial infections.

publication date

  • November 11, 2014

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed Central ID

  • PMC4234566

Digital Object Identifier (DOI)

  • 10.1073/pnas.1412487111

PubMed ID

  • 25355909

Additional Document Info

start page

  • 16059

end page

  • 64

volume

  • 111

number

  • 45