Cited by 357Inflammasome and immune disordersinterferon and immune responsesImmune Response and Inflammation

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Guanylate binding proteins promote caspase-11–dependent pyroptosis in response to cytoplasmic LPS

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Pilla, Danielle M., Hagar, Jon A., Haldar, Arun K., Mason, Ashley K., Degrandi, Daniel, Pfeffer, Klaus, Ernst, Robert K., Yamamoto, Masahiro, Miao, Edward A., Coers, Jörn·2014·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.1321700111PMC PMC4000848

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Abstract

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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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: Haldar, Arun K.
Degrandi, Daniel
Pfeffer, Klaus
Ernst, Robert K.
Yamamoto, Masahiro
Miao, Edward A.
Coers, Jörn
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
DOI: 10.1073/pnas.1321700111
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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Guanylate binding proteins promote caspase-11–dependent pyroptosis in response to cytoplasmic LPS

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