Interferon-induced guanylate-binding proteins promote cytosolic lipopolysaccharide detection by caspase-11

DNA Cell Biol. 2015 Jan;34(1):1-5. doi: 10.1089/dna.2014.2701.

Abstract

Lipopolysaccharide (LPS) from gram-negative bacteria is a classical pathogen-associated molecular pattern and a strong inducer of immune responses. While the detection of LPS on the cell surface and in the endosome by Toll-like receptor 4 (TLR4) has been studied for some time, it has only recently been discovered that LPS can also be sensed in the cytosol of cells by a noncanonical inflammasome pathway, resulting in the activation of the cysteine protease caspase-11. Intriguingly, activation of this pathway requires the production of interferons (IFNs) and the induction of a class of IFN-induced GTPases called guanylate-binding proteins (GBPs), which have previously been linked to cell-autonomous killing of intracellular microbes. In this study, we review the recent advances in our understanding of cytosolic LPS sensing and the function of mammalian GBPs.

Publication types

  • Review

MeSH terms

  • Animals
  • Caspases / physiology*
  • Caspases, Initiator
  • Cytoplasm / enzymology
  • Cytoplasm / immunology
  • GTP-Binding Proteins / physiology*
  • Humans
  • Immunity, Innate
  • Inflammasomes / physiology
  • Interferons / physiology*
  • Lipopolysaccharides / pharmacology*

Substances

  • Inflammasomes
  • Lipopolysaccharides
  • Interferons
  • Casp4 protein, mouse
  • Caspases
  • Caspases, Initiator
  • GTP-Binding Proteins