Redundant roles for inflammasome receptors NLRP3 and NLRC4 in host defense against Salmonella
Open accessAbstract
Intracellular pathogens and endogenous danger signals in the cytosol engage NOD-like receptors (NLRs), which assemble inflammasome complexes to activate caspase-1 and promote the release of proinflammatory cytokines IL-1β and IL-18. However, the NLRs that respond to microbial pathogens in vivo are poorly defined. We show that the NLRs NLRP3 and NLRC4 both activate caspase-1 in response to Salmonella typhimurium. Responding to distinct bacterial triggers, NLRP3 and NLRC4 recruited ASC and caspase-1 into a single cytoplasmic focus, which served as the site of pro–IL-1β processing. Consistent with an important role for both NLRP3 and NLRC4 in innate immune defense against S. typhimurium, mice lacking both NLRs were markedly more susceptible to infection. These results reveal unexpected redundancy among NLRs in host defense against intracellular pathogens in vivo.
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Pro-caspase-1 undergoes proximity-induced autoproteolysis, leading to active caspase-1 processing pro-IL-1β and pro-IL-18 into their mature forms and subsequent secretion.
“Pro-caspase-1 then undergoes proximity-induced autoproteolysis, which leads to active caspase-1 processing pro-IL-1β and pro-IL-18 into their mature forms IL-1β and IL-18 and the subsequent secretion of these cytokines [55, 58, 61–63]”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [63]
The introduction describes pro-caspase-1 dimerization and autoproteolytic cleavage on an inflammasome platform, and the Results show caspase-1-dependent processing and release of mature IL-1β. The Discussion reports IL-18 secretion but only suggests that ASC foci may be sites of IL-18 processing; it does not establish the claimed cleavage of pro-IL-18 into mature IL-18. (LLM, conf=0.78)
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Self-citation
- Authors
- Broz, P., Newton, K., Lamkanfi, M., Mariathasan, S., Dixit, V. M., & Monack, D. M.
- Affiliations
- Department of Microbiology and Immunology, Stanford School of Medicine, Stanford University, Stanford, CA 1
- Genentech (US)
- Stanford Medicine (US)
- Corresponding author
- Monack, Denise M.
- Venue
- Journal of Experimental Medicine
- Publisher
- Rockefeller University Press
- Published
- 2010-07-05
- Volume
- 207
- Issue
- 8
- Pages
- 1745-1755
- ISSN
- 0022-1007 (ISSN-L)
- 1540-9538
- PMC
- PMC2916133
- OpenAlex
- W2045953344
- Cited by
- 549
- References
- 6
- Citations by year
- 2026: 21 · 2025: 20 · 2024: 20 · 2023: 36 · 2022: 23 · 2021: 27 · 2020: 43 · 2019: 29 · 2018: 27 · 2017: 40 · 2016: 46 · 2015: 40 · 2014: 36 · 2013: 40 · 2012: 51
- FWCI
- 18.25
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Experimental Medicine (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Ghent University Academic Bibliography (Ghent University) (submittedVersion)
- Funders
- National Science Foundation
- Burroughs Wellcome Fund (AI063302)
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
- National Institutes of Health (AI063302)
- Genentech
- National Institute of Allergy and Infectious Diseases (AI063302, P01AI063302)
- 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 › Agricultural and Biological Sciences › Food Science › Salmonella and Campylobacter epidemiology
- Keywords
- NLRP3, NLRC4, NOD-like receptors, inflammasome, caspase-1, Salmonella typhimurium, IL-1β processing, ASC, innate immunity, intracellular pathogens, receptor redundancy, host defense
- MeSH terms
- NLR Family, Pyrin Domain-Containing 3 Protein, Animals, Animal Structures, Bacterial Proteins, Blood, Calcium-Binding Proteins, Carrier Proteins, Cytoskeletal Proteins, Flagellin, Immunity, Innate, Interleukin-1, Macrophages, Membrane Proteins, Mice, Inbred Strains, Protein Precursors, Salmonella Infections, Salmonella typhimurium, Cysteine Proteinase Inhibitors, Mice, Knockout, Models, Immunological, Caspase 1, Interleukin-18, Protein Transport, Cytoplasmic Structures, Apoptosis Regulatory Proteins, Mice, CARD Signaling Adaptor Proteins, Interleukin-1beta, Caspase Inhibitors
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