Salmonella-induced inflammasome activation in humans

Damien Bierschenk, Dave Boucher, Kate Schroder

Research output: Contribution to journalReview articlepeer-review


Inflammasomes are macromolecular complexes that assemble upon recognition of pathogen- or danger-associated molecular patterns. Inflammasome assembly is nucleated by the oligomerisation of specific, activated pattern recognition receptors within the cytosol. Inflammasomes function as platforms for the activation of the caspase-1 protease, which in turn triggers the maturation and secretion of the pro-inflammatory cytokines IL-1β and IL-18, and initiates pyroptosis, a highly inflammatory form of lytic cell death. Recently, additional inflammatory caspases (murine caspase-11, and human caspase-4/5) were also reported to be activated upon a pyroptosis-inducing 'non-canonical inflammasome' by direct recognition of lipopolysaccharide (LPS), a pathogen-associated molecular pattern. Here we review and discuss recent advances in our understanding of inflammasome-mediated host defence against Salmonella particularly in human cells, and their implications for cellular survival and cytokine secretion.

Original languageEnglish
Pages (from-to)38-43
Number of pages6
JournalMolecular immunology
Early online date11 Dec 2016
Publication statusE-pub ahead of print - 11 Dec 2016

Bibliographical note

Copyright © 2016 Elsevier Ltd. All rights reserved.


  • Animals
  • Caspases/metabolism
  • Host-Pathogen Interactions/immunology
  • Humans
  • Immunity, Innate
  • Inflammasomes/immunology
  • Interleukin-18/metabolism
  • Interleukin-1beta/metabolism
  • Intestinal Mucosa/immunology
  • Macrophages/immunology
  • Mice
  • NLR Proteins/metabolism
  • Pathogen-Associated Molecular Pattern Molecules/immunology
  • Pyroptosis
  • Salmonella Infections/immunology
  • Salmonella typhimurium/immunology
  • Signal Transduction
  • Toll-Like Receptors/metabolism

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