Guanylate-binding proteins promote activation of the AIM2 inflammasome during infection with Francisella novicida View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2015-05

AUTHORS

Etienne Meunier, Pierre Wallet, Roland F Dreier, Stéphanie Costanzo, Leonie Anton, Sebastian Rühl, Sébastien Dussurgey, Mathias S Dick, Anne Kistner, Mélanie Rigard, Daniel Degrandi, Klaus Pfeffer, Masahiro Yamamoto, Thomas Henry, Petr Broz

ABSTRACT

The AIM2 inflammasome detects double-stranded DNA in the cytosol and induces caspase-1-dependent pyroptosis as well as release of the inflammatory cytokines interleukin 1β (IL-1β) and IL-18. AIM2 is critical for host defense against DNA viruses and bacteria that replicate in the cytosol, such as Francisella tularensis subspecies novicida (F. novicida). The activation of AIM2 by F. novicida requires bacteriolysis, yet whether this process is accidental or is a host-driven immunological mechanism has remained unclear. By screening nearly 500 interferon-stimulated genes (ISGs) through the use of small interfering RNA (siRNA), we identified guanylate-binding proteins GBP2 and GBP5 as key activators of AIM2 during infection with F. novicida. We confirmed their prominent role in vitro and in a mouse model of tularemia. Mechanistically, these two GBPs targeted cytosolic F. novicida and promoted bacteriolysis. Thus, in addition to their role in host defense against vacuolar pathogens, GBPs also facilitate the presentation of ligands by directly attacking cytosolic bacteria. More... »

PAGES

476-484

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ni.3119

DOI

http://dx.doi.org/10.1038/ni.3119

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1000522950

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/25774716


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