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000284081 041__ $$aEnglish
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000284081 1001_ $$00000-0002-9495-706X$$aBertheloot, Damien$$b0
000284081 245__ $$aNanobodies dismantle post‐pyroptotic ASC specks and counteract inflammation in vivo
000284081 260__ $$a[London]$$bNature Publishing Group UK$$c2022
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000284081 520__ $$aInflammasomes sense intracellular clues of infection, damage, or metabolic imbalances. Activated inflammasome sensors polymerize the adaptor ASC into micron-sized 'specks' to maximize caspase-1 activation and the maturation of IL-1 cytokines. Caspase-1 also drives pyroptosis, a lytic cell death characterized by leakage of intracellular content to the extracellular space. ASC specks are released among cytosolic content, and accumulate in tissues of patients with chronic inflammation. However, if extracellular ASC specks contribute to disease, or are merely inert remnants of cell death remains unknown. Here, we show that camelid-derived nanobodies against ASC (VHHASC ) target and disassemble post-pyroptotic inflammasomes, neutralizing their prionoid, and inflammatory functions. Notably, pyroptosis-driven membrane perforation and exposure of ASC specks to the extracellular environment allowed VHHASC to target inflammasomes while preserving pre-pyroptotic IL-1β release, essential to host defense. Systemically administrated mouse-specific VHHASC attenuated inflammation and clinical gout, and antigen-induced arthritis disease. Hence, VHHASC neutralized post-pyroptotic inflammasomes revealing a previously unappreciated role for these complexes in disease. VHHASC are the first biologicals that disassemble pre-formed inflammasomes while preserving their functions in host defense.
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000284081 650_7 $$2Other$$aarthritis
000284081 650_7 $$2Other$$aextracellular inflammasomes
000284081 650_7 $$2Other$$agout
000284081 650_7 $$2Other$$ananobodies
000284081 650_7 $$2Other$$apyroptosis
000284081 650_7 $$2NLM Chemicals$$aCARD Signaling Adaptor Proteins
000284081 650_7 $$2NLM Chemicals$$aInflammasomes
000284081 650_7 $$2NLM Chemicals$$aNLR Family, Pyrin Domain-Containing 3 Protein
000284081 650_7 $$2NLM Chemicals$$aSingle-Domain Antibodies
000284081 650_7 $$0EC 3.4.22.36$$2NLM Chemicals$$aCaspase 1
000284081 650_2 $$2MeSH$$aAnimals
000284081 650_2 $$2MeSH$$aCARD Signaling Adaptor Proteins: metabolism
000284081 650_2 $$2MeSH$$aCaspase 1: metabolism
000284081 650_2 $$2MeSH$$aHumans
000284081 650_2 $$2MeSH$$aInflammasomes: metabolism
000284081 650_2 $$2MeSH$$aInflammation: metabolism
000284081 650_2 $$2MeSH$$aMice
000284081 650_2 $$2MeSH$$aNLR Family, Pyrin Domain-Containing 3 Protein: metabolism
000284081 650_2 $$2MeSH$$aPyroptosis
000284081 650_2 $$2MeSH$$aSingle-Domain Antibodies
000284081 7001_ $$aWanderley, Carlos WS$$b1
000284081 7001_ $$aSchneider, Ayda H$$b2
000284081 7001_ $$00000-0003-2301-1610$$aSchiffelers, Lisa DJ$$b3
000284081 7001_ $$00000-0002-3391-9633$$aWuerth, Jennifer D$$b4
000284081 7001_ $$00000-0002-9104-5858$$aTödtmann, Jan MP$$b5
000284081 7001_ $$00000-0002-4615-7252$$aMaasewerd, Salie$$b6
000284081 7001_ $$aHawwari, Ibrahim$$b7
000284081 7001_ $$aDuthie, Fraser$$b8
000284081 7001_ $$aRohland, Cornelia$$b9
000284081 7001_ $$0P:(DE-2719)9001782$$aSecchim Ribeiro, Lucas$$b10$$udzne
000284081 7001_ $$00000-0001-8580-4590$$aJenster, Lea-Marie$$b11
000284081 7001_ $$aRosero, Nathalia$$b12
000284081 7001_ $$00000-0003-0106-7277$$aTesfamariam, Yonas M$$b13
000284081 7001_ $$aCunha, Fernando Q$$b14
000284081 7001_ $$00000-0002-9979-9769$$aSchmidt, Florian I$$b15
000284081 7001_ $$aFranklin, Bernardo S$$b16
000284081 773__ $$0PERI:(DE-600)2485479-7$$a10.15252/emmm.202115415$$gVol. 14, no. 6, p. e15415$$n6$$pe15415$$tEMBO molecular medicine$$v14$$x1757-4676$$y2022
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