| First Author | Man SM | Year | 2013 |
| Journal | J Immunol | Volume | 191 |
| Issue | 10 | Pages | 5239-46 |
| PubMed ID | 24123685 | Mgi Jnum | J:206327 |
| Mgi Id | MGI:5550029 | Doi | 10.4049/jimmunol.1301581 |
| Citation | Man SM, et al. (2013) Salmonella infection induces recruitment of Caspase-8 to the inflammasome to modulate IL-1beta production. J Immunol 191(10):5239-46 |
| abstractText | Nucleotide-binding oligomerization domain-like receptors (NLRs) detect pathogens and danger-associated signals within the cell. Salmonella enterica serovar Typhimurium, an intracellular pathogen, activates caspase-1 required for the processing of the proinflammatory cytokines, pro-IL-1beta and pro-IL-18, and pyroptosis. In this study, we show that Salmonella infection induces the formation of an apoptosis-associated specklike protein containing a CARD (ASC)-Caspase-8-Caspase-1 inflammasome in macrophages. Caspase-8 and caspase-1 are recruited to the ASC focus independently of one other. Salmonella infection initiates caspase-8 proteolysis in a manner dependent on NLRC4 and ASC, but not NLRP3, caspase-1 or caspase-11. Caspase-8 primarily mediates the synthesis of pro-IL-1beta, but is dispensable for Salmonella-induced cell death. Overall, our findings highlight that the ASC inflammasome can recruit different members of the caspase family to induce distinct effector functions in response to Salmonella infection. |
