PMC:7103735 / 42366-45706 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7103735","sourcedb":"PMC","sourceid":"7103735","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7103735","text":"One form of cell death known as pyroptosis is one of the results of a proinflammatory cytokine storm, which drives at least in part the high pathogenicity of SARS-CoV and MERS-CoV. Poor outcomes of patients with SARS and MERS are often associated with exceedingly high levels of proinflammatory cytokines in the lower respiratory tract and other tissues [71]. The upregulation of inflammatory cytokines, including interleukin (IL) 1β, was observed in SARS-CoV-infected monocyte-derived human dendritic cells and tissue models [72]. Maturation of IL-1β is generated through proteolytic cleavage of pro-IL-1β by caspase 1, the activation of which requires the formation of a multiprotein complex termed inflammasome. When danger signals are sensed in the cells, NLRP3 is activated to recruit ASC and facilitate its oligomerization. For full activation of inflammasome activity, two signals that, respectively, stimulate pro-IL-1β transcription (signal 1) and cleave pro-IL-1β (signal 2) are required. Recombinant SARS-CoVs with either deletion of ORF3a or defective ion channel activity of E protein are compromised in the activation of IL-1β maturation and secretion [73,74]. Mechanistically, both ORF3a and E can activate both signals. Both stimulates NF-κB activation, resulting in the activation of pro-IL-1β transcription [73,75]. In particular, ORF3a achieves this through TRAF3-dependent ubiquitination of p105 [73]. For the activation of the second signal, ion channel activity of SARS-CoV E protein promotes assembly of NLRP3 inflammasome [76]. Different mechanisms have been suggested for SARS-CoV ORF3a-mediated inflammasome activation. We demonstrated that SARS-CoV ORF3a promotes NLRP3 inflammasome assembly through TRAF3-dependent K63 ubiquitination of ASC [73]. Alternatively, SARS-CoV ORF3a might provide a potassium flux through its ion channel domain to activate NEK7-dependent NLRP3 inflammasome [77]. Further investigations are required to resolve the discrepancies (Figure 2). Nevertheless, enhanced secretion of IL-1β mediated by SARS-CoV E and ORF3a proteins might contribute to the induction of proinflammatory cytokine storm since IL-1β further promotes the expression of other proinflammatory cytokines such as tumour necrosis factor α and IL-6 [74,75]. Thus, small-molecule inhibitors of NLRP3 inflammasomes such as MCC950 and INF58 might prove useful in the treatment of COVID-19. This merits further preclinical and clinical studies.\nFigure 2. A working model of SARS-CoV-induced inflammasome activation. SARS-CoV can activate both signal 1 (priming) and signal 2 (activation). Upregulation of pro-IL-1β transcription is achieved by NF-κB activation. Two mechanisms of IL-1β maturation have been proposed. In the first model, potassium ion efflux is promoted by ORF3a and E proteins, leading to NLRP3 inflammasome assembly. Alternatively, ORF3a promotes ASC ubiquitination and consequent assembly of inflammasome. ORG8b interacts with and activates NLRP3. Activation of inflammasome leads to proteolytic cleavage of pro-caspase 1 and pro-IL-1β. ASC, apoptosis-associated speck-like protein containing a CARD. CASP1, caspase 1. IKK, IκB kinase. IL-1, interleukin-1. LPS, lipopolysaccharides. NLRP3, NACHT, LRR, and PYD domains-containing protein 3. NEMO, NF-κB essential modulator. 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