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@ARTICLE{Bertheloot:284081,
author = {Bertheloot, Damien and Wanderley, Carlos WS and Schneider,
Ayda H and Schiffelers, Lisa DJ and Wuerth, Jennifer D and
Tödtmann, Jan MP and Maasewerd, Salie and Hawwari, Ibrahim
and Duthie, Fraser and Rohland, Cornelia and Secchim
Ribeiro, Lucas and Jenster, Lea-Marie and Rosero, Nathalia
and Tesfamariam, Yonas M and Cunha, Fernando Q and Schmidt,
Florian I and Franklin, Bernardo S},
title = {{N}anobodies dismantle post‐pyroptotic {ASC} specks and
counteract inflammation in vivo},
journal = {EMBO molecular medicine},
volume = {14},
number = {6},
issn = {1757-4676},
address = {[London]},
publisher = {Nature Publishing Group UK},
reportid = {DZNE-2026-00089},
pages = {e15415},
year = {2022},
abstract = {Inflammasomes 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.},
keywords = {Animals / CARD Signaling Adaptor Proteins: metabolism /
Caspase 1: metabolism / Humans / Inflammasomes: metabolism /
Inflammation: metabolism / Mice / NLR Family, Pyrin
Domain-Containing 3 Protein: metabolism / Pyroptosis /
Single-Domain Antibodies / arthritis (Other) / extracellular
inflammasomes (Other) / gout (Other) / nanobodies (Other) /
pyroptosis (Other) / CARD Signaling Adaptor Proteins (NLM
Chemicals) / Inflammasomes (NLM Chemicals) / NLR Family,
Pyrin Domain-Containing 3 Protein (NLM Chemicals) /
Single-Domain Antibodies (NLM Chemicals) / Caspase 1 (NLM
Chemicals)},
ddc = {610},
pnm = {899 - ohne Topic (POF4-899)},
pid = {G:(DE-HGF)POF4-899},
typ = {PUB:(DE-HGF)16},
doi = {10.15252/emmm.202115415},
url = {https://pub.dzne.de/record/284081},
}