The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.
Nitric oxide controls the immunopathology of tuberculosis by inhibiting NLRP3 inflammasome–dependent processing of IL-1β
Open accessAbstract
Interleukin 1 (IL-1) is an important mediator of innate immunity but can also promote inflammatory tissue damage. During chronic infections such as tuberculosis, the beneficial antimicrobial role of IL-1 must be balanced with the need to prevent immunopathology. By exogenously controlling the replication of Mycobacterium tuberculosis in vivo, we obviated the requirement for antimicrobial immunity and discovered that both IL-1 production and infection-induced immunopathology were suppressed by lymphocyte-derived interferon-γ (IFN-γ). This effect was mediated by nitric oxide (NO), which we found specifically inhibited assembly of the NLRP3 inflammasome via thiol nitrosylation. Our data indicate that the NO produced as a result of adaptive immunity is indispensable in modulating the destructive innate inflammatory responses elicited during persistent infections.
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“Similarly, NO directly blocks inflammasome activation via nitrosylation of NLRP3, thereby preventing excessive tissue damage in the course of M. tuberculosis infection (102, 103).”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [103]
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NLRP3 inflammasomes are required for atherogenesis and activated by cholesterol crystals
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Self-citationImmunological and inflammatory functions of the interleukin-1 family
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AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC
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Regulation of inflammasome signaling
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Self-citationThe Biotin Switch Method for the Detection of S -Nitrosylated Proteins
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Reactive oxygen species and mitochondria: A nexus of cellular homeostasis
Dunn, J. D., Álvarez, L., Zhang, X., & Soldati, T. (2015) · Redox Biology · doi:10.1016/j.redox.2015.09.005 · Cited by 1,233
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Metadata
- Authors
- Mishra, B. B., Rathinam, V. A. K., Martens, G. W., Martinot, A. J., Kornfeld, H., Fitzgerald, K. A., & Sassetti, C. M.
- Affiliations
- University of Massachusetts Chan Medical School (US)
- Harvard University (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Sassetti, Christopher M
- ORCID
- Venue
- Nature Immunology
- Published
- 2012-11-18
- Volume
- 14
- Issue
- 1
- Pages
- 52-60
- ISSN
- 1529-2908 (ISSN-L)
- 1529-2916
- PMC
- PMC3721324
- OpenAlex
- W2048884877
- Cited by
- 571
- References
- 49
- Citations by year
- 2026: 24 · 2025: 27 · 2024: 29 · 2023: 39 · 2022: 47 · 2021: 53 · 2020: 46 · 2019: 43 · 2018: 51 · 2017: 46 · 2016: 46 · 2015: 40 · 2014: 40 · 2013: 37 · 2012: 3
- FWCI
- 15.44
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Immunology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Howard Hughes Medical Institute
- National Heart, Lung, and Blood Institute (R01HL064884, R01HL081149, HL064884)
- National Institute of Allergy and Infectious Diseases (AI064282, R01AI064282, AI083713, U54AI057159, R01AI083713, T32AI007638)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- nitric oxide, NLRP3 inflammasome, interleukin-1β processing, tuberculosis, immunopathology, Mycobacterium tuberculosis, nitrosylation, interferon-gamma, innate immunity, chronic infection, adaptive immunity
- MeSH terms
- NLR Family, Pyrin Domain-Containing 3 Protein, Animals, Carrier Proteins, Cells, Cultured, Humans, Immunity, Innate, Interferon-gamma, Mice, Inbred C57BL, Mycobacterium tuberculosis, Nitric Oxide, Tuberculosis, Signal Transduction, Mice, Knockout, Protein Modification, Translational, Mice, Interleukin-1beta, Protein Multimerization, Inflammasomes
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