{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,22]],"date-time":"2026-07-22T02:59:03Z","timestamp":1784689143249,"version":"3.55.0"},"reference-count":193,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2022,8,30]],"date-time":"2022-08-30T00:00:00Z","timestamp":1661817600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000925","name":"National Health and Medical Research Council","doi-asserted-by":"publisher","award":["1157053"],"award-info":[{"award-number":["1157053"]}],"id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Immunol."],"abstract":"<jats:p>The innate immune response to viruses is critical for the correct establishment of protective adaptive immunity. Amongst the many pathways involved, the NLRP3 [nucleotide-binding oligomerisation domain (NOD)-like receptor protein 3 (NLRP3)] inflammasome has received considerable attention, particularly in the context of immunity and pathogenesis during infection with influenza A (IAV) and SARS-CoV-2, the causative agent of COVID-19. Activation of the NLRP3 inflammasome results in the secretion of the proinflammatory cytokines IL-1\u03b2 and IL-18, commonly coupled with pyroptotic cell death. While this mechanism is protective and key to host defense, aberrant NLRP3 inflammasome activation causes a hyperinflammatory response and excessive release of cytokines, both locally and systemically. Here, we discuss key molecules in the NLRP3 pathway that have also been shown to have significant roles in innate and adaptive immunity to viruses, including DEAD box helicase X-linked (DDX3X), vimentin and macrophage migration inhibitory factor (MIF). We also discuss the clinical opportunities to suppress NLRP3-mediated inflammation and reduce disease severity.<\/jats:p>","DOI":"10.3389\/fimmu.2022.987453","type":"journal-article","created":{"date-parts":[[2022,8,30]],"date-time":"2022-08-30T06:24:03Z","timestamp":1661840643000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":29,"title":["The multifaceted roles of NLRP3-modulating proteins in virus infection"],"prefix":"10.3389","volume":"13","author":[{"given":"James","family":"Harris","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Natalie A.","family":"Borg","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2022,8,30]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","DOI":"10.1016\/j.antiviral.2020.104742","article-title":"The spike glycoprotein of the new coronavirus 2019-nCoV contains a furin-like cleavage site absent in CoV of the same clade","volume":"176","author":"Coutard","year":"2020","journal-title":"Antiviral Res"},{"key":"B2","doi-asserted-by":"publisher","DOI":"10.1016\/j.cell.2020.02.052","article-title":"SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor","volume":"181","author":"Hoffmann","year":"2020","journal-title":"Cell"},{"key":"B3","doi-asserted-by":"publisher","DOI":"10.1016\/j.isci.2020.101212","article-title":"Proteolytic cleavage of the SARS-CoV-2 spike protein and the role of the novel S1\/S2 site","volume":"23","author":"Jaimes","year":"2020","journal-title":"iScience"},{"key":"B4","doi-asserted-by":"publisher","DOI":"10.1038\/s41401-020-0485-4","article-title":"Structural and functional properties of SARS-CoV-2 spike protein: potential antivirus drug development for COVID-19","volume":"41","author":"Huang","year":"2020","journal-title":"Acta Pharmacol Sin"},{"key":"B5","doi-asserted-by":"publisher","DOI":"10.1016\/j.cell.2020.09.033","article-title":"SARS-CoV-2 infection depends on cellular heparan sulfate and ACE2","volume":"183","author":"Clausen","year":"2020","journal-title":"Cell"},{"key":"B6","doi-asserted-by":"publisher","DOI":"10.1038\/s41392-020-00426-x","article-title":"CD147-spike protein is a novel route for SARS-CoV-2 infection to host cells","volume":"5","author":"Wang","year":"2020","journal-title":"Signal Transduct Target Ther"},{"key":"B7","doi-asserted-by":"publisher","DOI":"10.1126\/science.abd2985","article-title":"Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity","volume":"370","author":"Cantuti-Castelvetri","year":"2020","journal-title":"Science"},{"key":"B8","doi-asserted-by":"publisher","DOI":"10.1021\/acscentsci.0c01537","article-title":"CD209L\/L-SIGN and CD209\/DC-SIGN act as receptors for SARS-CoV-2","volume":"7","author":"Amraei","year":"2021","journal-title":"ACS Cent Sci"},{"key":"B9","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.78.11.5642-5650.2004","article-title":"pH-dependent entry of severe acute respiratory syndrome coronavirus is mediated by the spike glycoprotein and enhanced by dendritic cell transfer through DC-SIGN","volume":"78","author":"Yang","year":"2004","journal-title":"J Virol"},{"key":"B10","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0403812101","article-title":"CD209L (L-SIGN) is a receptor for severe acute respiratory syndrome coronavirus","volume":"101","author":"Jeffers","year":"2004","journal-title":"Proc Natl Acad Sci U.S.A."},{"key":"B11","doi-asserted-by":"publisher","DOI":"10.1038\/s41586-021-03925-1","article-title":"Lectins enhance SARS-CoV-2 infection and influence neutralizing antibodies","volume":"598","author":"Lempp","year":"2021","journal-title":"Nature"},{"key":"B12","doi-asserted-by":"publisher","DOI":"10.3389\/fimmu.2018.01581","article-title":"Influenza a virus cell entry, replication, virion assembly and movement","volume":"9","author":"Dou","year":"2018","journal-title":"Front Immunol"},{"key":"B13","doi-asserted-by":"publisher","DOI":"10.1016\/j.coviro.2021.03.001","article-title":"Entry of influenza a virus into host cells - 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