Research output: Contribution to journal › Review article › peer-review
Journal | Molecular immunology |
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Date | Accepted/In press - 17 Nov 2016 |
Date | E-pub ahead of print (current) - 11 Dec 2016 |
Volume | 86 |
Number of pages | 6 |
Pages (from-to) | 38-43 |
Early online date | 11/12/16 |
Original language | English |
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.
Copyright © 2016 Elsevier Ltd. All rights reserved.
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