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• W4385157056 startingPage "156302" @default.
• W4385157056 abstract "Gram-positive bacterial infection causes high morbidity and mortality worldwide, while the underlying mechanism for host sensing bacterial components and initiating immune responses remains elusive. The NLRP3 inflammasome is a cytosolic multi-protein complex sensing a broad spectrum of endogenous danger signals and environmental irritants. In contrast to canonical NLRP3 inflammasome activation that needs both priming and activation signals, Lipopolysaccharide (LPS) from gram-negative bacteria activates the one-step NLRP3 inflammasome in human monocytes, which relies on the TLR4-TRIF-Caspase-8 signaling. Here, we show that in human monocytes, TLR2 agonists such as heat-killed gram-positive bacteria, peptidoglycan (PGN) or synthetic bacterial lipoprotein analog Pam3CysSerLys4 (Pam3CSK4) are able to induce the one-step NLRP3 inflammasome activation. Using genetic targeting and pharmacological inhibition approaches, it was found that TLR2 propagates signal through TRAF6, TAK1 and IKKβ, ultimately activated NLRP3 independent of RelA. In addition, IKKβ interacts with NLRP3 directly and affects NLRP3 inflammasome activation. These results reveal the signaling cascade downstream of TLR2 upon sensing gram-positive bacterial infection and activating the one-step NLRP3 inflammasome in human monocytes, which provides clue for controlling gram-positive bacterial infection-related inflammation." @default.
• W4385157056 created "2023-07-24" @default.
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• W4385157056 date "2023-09-01" @default.
• W4385157056 modified "2023-10-12" @default.
• W4385157056 title "TRAF6-TAK1-IKKβ pathway mediates TLR2 agonists activating “one-step” NLRP3 inflammasome in human monocytes" @default.
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• W4385157056 doi "https://doi.org/10.1016/j.cyto.2023.156302" @default.
• W4385157056 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/37480791" @default.
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