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Guanylate binding proteins promote caspase-11–dependent pyroptosis in response to cytoplasmic LPS
Open accessAbstract
Significance: A major component of the cell envelope of Gram-negative bacteria is LPS, also known as endotoxin. LPS produced during bacterial infections triggers inflammation, which can lead to septic shock and death. Our immune system can recognize LPS both outside and inside of cells. The recognition of extracellular and vacuolar LPS by LPS binding proteins is well described, but little is known about the recognition of cytoplasmic LPS. Here, we show that cytoplasmic LPS derived from the intracellular bacterial pathogen Legionella activated a proinflammatory immune response. We further identified host guanylate binding proteins as critical mediators of immunity triggered by cytoplasmic LPS. These findings are likely to advance our understanding of how cells can sense intracellular LPS.
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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 [647]
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Metadata
- Authors
- Pilla, D. M., Hagar, J. A., Haldar, A. K., Mason, A. K., Degrandi, D., Pfeffer, K., Ernst, R. K., Yamamoto, M., Miao, E. A., & Coers, J.
- Affiliations
- Duke University (US)
- University of North Carolina at Chapel Hill (US)
- University of Maryland, Baltimore (US)
- Heinrich Heine University Düsseldorf (DE)
- The University of Osaka (JP)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2014-04-08
- Volume
- 111
- Issue
- 16
- Pages
- 6046-6051
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC4000848
- OpenAlex
- W1984035213
- Cited by
- 357
- References
- 43
- Citations by year
- 2026: 20 · 2025: 28 · 2024: 24 · 2023: 27 · 2022: 32 · 2021: 22 · 2020: 42 · 2019: 32 · 2018: 26 · 2017: 30 · 2016: 31 · 2015: 31 · 2014: 11
- FWCI
- 14.07
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Heart Association (12PRE10440003)
- Deutsche Forschungsgemeinschaft (FOR729)
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases (R21AI099823, R01AI103197, R01AI097518, U54AI057157, R37AI103197)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- guanylate-binding proteins, caspase-11, pyroptosis, non-canonical inflammasome, Legionella pneumophila, cell-autonomous immunity, macrophages, interferon signaling, Escherichia coli LPS, intracellular bacterial infection
- MeSH terms
- NADPH Oxidase 2, Animals, Cytoplasm, Enzyme Activation, Interferon-gamma, Legionnaires' Disease, Lipopolysaccharides, Macrophage Activation, Macrophages, Membrane Glycoproteins, Mice, Inbred C57BL, Mutation, Salmonella typhimurium, Legionella pneumophila, Apoptosis, GTP-Binding Proteins, NADPH Oxidases, Caspases, Mice, Nitric Oxide Synthase Type II, Caspases, Initiator
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