The role of the NLRP3 inflammasome in regulation of antiviral responses to influenza A virus infection

The innate immune system provides the host with both a dynamic barrier to prevent infection and a means to which rapid anti-microbial responses can be mounted. The inflammasome pathway is a critical host early response mechanism that enables detection of pathogens and initiates production of inflammatory cytokines, inducing recruitment of effector cells to the site of infection. The complete mechanism of inflammasome activation requires two signals: an initial priming step upon detection of pathogen, followed by activation of intracellular pattern recognition receptors critical to the formation of the inflammasome complex. The inflammasome complex is made of intracellular multiprotein oligomers which includes a sensor protein such as the nucleotide-binding oligomerization domain (NOD) like receptor proteins (NLRP), and an adapter protein, ASC, which critically activates pro-caspase-1. The mature caspase-1 then proteolytically cleaves cytosolic pro-IL-1β and pro-IL-18, which are then secreted as inflammatory cytokines that activate the inflammatory arm of the immune response to infection. Active caspase-1 also results in pyroptosis, which is a form of cell death triggered by inflammation. The induction and activation of IL-1β and IL-18 are considered critical signatures for inflammasome activation. With focus upon influenza A virus infection, this review will address present knowledge on the mechanisms of inflammasome complex activation, particularly how the viral components modulate activation of the cytosolic NOD-like receptor protein-3 (NLRP3)-dependent inflammasome complex. We also discuss potential therapeutic strategies that target the inflammasome to ameliorate illness, as well as novel methods of vaccination that target inflammasome stimulation with the aim to increase efficacy.