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IRGB10 Liberates Bacterial Ligands for Sensing by the AIM2 and Caspase-11-NLRP3 Inflammasomes
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The inflammasome is an intracellular signaling complex, which on recognition of pathogens and physiological aberration, drives activation of caspase-1, pyroptosis, and the release of the pro-inflammatory cytokines IL-1β and IL-18. Bacterial ligands must secure entry into the cytoplasm to activate inflammasomes; however, the mechanisms by which concealed ligands are liberated in the cytoplasm have remained unclear. Here, we showed that the interferon-inducible protein IRGB10 is essential for activation of the DNA-sensing AIM2 inflammasome by Francisella novicida and contributed to the activation of the LPS-sensing caspase-11 and NLRP3 inflammasome by Gram-negative bacteria. IRGB10 directly targeted cytoplasmic bacteria through a mechanism requiring guanylate-binding proteins. Localization of IRGB10 to the bacterial cell membrane compromised bacterial structural integrity and mediated cytosolic release of ligands for recognition by inflammasome sensors. Overall, our results reveal IRGB10 as part of a conserved signaling hub at the interface between cell-autonomous immunity and innate immune sensing pathways.
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“(3) the expression of guanylate-binding proteins and an IFN-inducible GTPase commonly known as IRGB10 (official name Gm12250), which increase cytosolic LPS levels by mediating the lysis of vacuoles containing Gram-negative bacteria [646–648].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [648]
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Metadata
- Authors
- Man, S. M., Karki, R., Sasai, M., Place, D. E., Kesavardhana, S., Temirov, J., Frase, S., Zhu, Q., Malireddi, R. K. S., Kuriakose, T., Peters, J. L., Neale, G., Brown, S. A., Yamamoto, M., & Kanneganti, T.-D.
- Affiliations
- St. Jude Children's Research Hospital (US)
- Immunology Frontier Research Center, The University of Osaka (JP)
- Corresponding author
- Kanneganti, Thirumala-Devi
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2016-10
- Volume
- 167
- Issue
- 2
- Pages
- 382-396.e17
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC5074697
- OpenAlex
- W2524431814
- Cited by
- 312
- References
- 57
- Citations by year
- 2026: 12 · 2025: 35 · 2024: 18 · 2023: 28 · 2022: 32 · 2021: 30 · 2020: 49 · 2019: 37 · 2018: 31 · 2017: 37 · 2016: 2
- FWCI
- 18.53
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Seoul National University Open Repository (Seoul National University) (submittedVersion)
- Funders
- National Cancer Institute (R01CA163507, P30CA021765)
- National Institute of Allergy and Infectious Diseases (R01AI101935, R37AI101935, R01AI124346)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR056296)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Keywords
- AIM2 inflammasome, caspase-11, NLRP3 inflammasome, Francisella novicida, Gram-negative bacteria, guanylate-binding proteins, plasma membrane targeting, DNA sensing, pyroptosis, IL-1β, IL-18, cell-autonomous immunity, innate immune recognition
- MeSH terms
- NLR Family, Pyrin Domain-Containing 3 Protein, Animals, B-Lymphocytes, Cytosol, DNA-Binding Proteins, Francisella, Immunity, Cellular, Immunity, Innate, Ligands, Mice, Mutant Strains, T-Lymphocytes, Gram-Negative Bacterial Infections, Caspases, GTP Phosphohydrolases, Myeloid Cells, Mice, Caspases, Initiator, Host-Pathogen Interactions, Inflammasomes
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