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http://purl.uniprot.org/citations/28331908http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28331908http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28331908http://www.w3.org/2000/01/rdf-schema#comment"Interleukin-1β (IL-1β) is a key proinflammatory cytokine that drives antimicrobial immune responses. IL-1β is aberrantly activated in autoimmune diseases, and IL-1β inhibitors are used as therapeutic agents to treat patients with certain autoimmune disorders. Review of postmarketing surveillance of patients receiving IL-1β inhibitors found a disproportionate reporting of invasive infections by group A Streptococcus (GAS). IL-1β inhibition increased mouse susceptibility to GAS infection, but IL-1β was produced independent of canonical inflammasomes. Newly synthesized IL-1β has an amino-terminal prodomain that blocks signaling activity, which is usually proteolytically removed by caspase-1, a protease activated within the inflammasome structure. In place of host caspases, the secreted GAS cysteine protease SpeB generated mature IL-1β. During invasive infection, GAS isolates may acquire pathoadaptive mutations eliminating SpeB expression to evade detection by IL-1β. Pharmacological IL-1β inhibition alleviates this selective pressure, allowing invasive infection by nonpathoadapted GAS. Thus, IL-1β is a sensor that directly detects pathogen-associated proteolysis through an independent pathway operating in parallel with host inflammasomes. Because IL-1β function is maintained across species, yet cleavage by caspases does not appear to be, detection of microbial proteases may represent an ancestral system of innate immune regulation."xsd:string
http://purl.uniprot.org/citations/28331908http://purl.org/dc/terms/identifier"doi:10.1126/sciimmunol.aah3539"xsd:string
http://purl.uniprot.org/citations/28331908http://purl.org/dc/terms/identifier"doi:10.1126/sciimmunol.aah3539"xsd:string
http://purl.uniprot.org/citations/28331908http://purl.uniprot.org/core/author"Olson J."xsd:string
http://purl.uniprot.org/citations/28331908http://purl.uniprot.org/core/author"Olson J."xsd:string
http://purl.uniprot.org/citations/28331908http://purl.uniprot.org/core/author"Todd J."xsd:string
http://purl.uniprot.org/citations/28331908http://purl.uniprot.org/core/author"Todd J."xsd:string
http://purl.uniprot.org/citations/28331908http://purl.uniprot.org/core/author"Nizet V."xsd:string
http://purl.uniprot.org/citations/28331908http://purl.uniprot.org/core/author"Nizet V."xsd:string
http://purl.uniprot.org/citations/28331908http://purl.uniprot.org/core/author"Cooper M.A."xsd:string
http://purl.uniprot.org/citations/28331908http://purl.uniprot.org/core/author"Cooper M.A."xsd:string
http://purl.uniprot.org/citations/28331908http://purl.uniprot.org/core/author"Robertson A.A."xsd:string
http://purl.uniprot.org/citations/28331908http://purl.uniprot.org/core/author"Robertson A.A."xsd:string
http://purl.uniprot.org/citations/28331908http://purl.uniprot.org/core/author"O'Donoghue A.J."xsd:string
http://purl.uniprot.org/citations/28331908http://purl.uniprot.org/core/author"O'Donoghue A.J."xsd:string
http://purl.uniprot.org/citations/28331908http://purl.uniprot.org/core/author"Hoffman H.M."xsd:string
http://purl.uniprot.org/citations/28331908http://purl.uniprot.org/core/author"Hoffman H.M."xsd:string
http://purl.uniprot.org/citations/28331908http://purl.uniprot.org/core/author"LaRock C.N."xsd:string
http://purl.uniprot.org/citations/28331908http://purl.uniprot.org/core/author"LaRock C.N."xsd:string
http://purl.uniprot.org/citations/28331908http://purl.uniprot.org/core/author"LaRock D.L."xsd:string
http://purl.uniprot.org/citations/28331908http://purl.uniprot.org/core/author"LaRock D.L."xsd:string
http://purl.uniprot.org/citations/28331908http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/28331908http://purl.uniprot.org/core/date"2016"xsd:gYear