Cited by 403Inflammasome and immune disordersImmune Response and InflammationCell death mechanisms and regulation

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Pyroptosis triggers pore-induced intracellular traps (PITs) that capture bacteria and lead to their clearance by efferocytosis

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Jorgensen, Ine, Zhang, Yue, Krantz, Bryan A., Miao, Edward A.·2016·Journal of Experimental Medicine

DOI 10.1084/jem.20151613PMC PMC5030797

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Abstract

Inflammasomes activate caspase-1 in response to cytosolic contamination or perturbation. This inflammatory caspase triggers the opening of the GSDMD pore in the plasma membrane, resulting in lytic cell death called pyroptosis. We had previously assumed that pyroptosis releases intracellular bacteria to the extracellular space. Here, we find that viable bacteria instead remain trapped within the cellular debris of pyroptotic macrophages. This trapping appears to be an inevitable consequence of how osmotic lysis ruptures the plasma membrane, and may also apply to necroptosis and some forms of nonprogrammed necrosis. Although membrane tears release soluble cytosolic contents, they are small enough to retain organelles and bacteria. We call this structure the pore-induced intracellular trap (PIT), which is conceptually parallel to the neutrophil extracellular trap (NET). The PIT coordinates innate immune responses via complement and scavenger receptors to drive recruitment of and efferocytosis by neutrophils. Ultimately, this secondary phagocyte kills the bacteria. Hence, caspase-1–driven pore-induced cell death triggers a multifaceted defense against intracellular bacteria facilitated by trapping the pathogen within the cellular debris. Bona fide intracellular bacterial pathogens, such as Salmonella, must prevent or delay pyroptosis to avoid being trapped in the PIT and subsequently killed by neutrophils.

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Authors: Jorgensen, I., Zhang, Y., Krantz, B. A., & Miao, E. A.
Affiliations: Department of Microbiology and Immunology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599 1
University of North Carolina at Chapel Hill (US)
University of Maryland, Baltimore (US)
Corresponding author: Miao, Edward A.
ORCID: Jorgensen, Ine
Zhang, Yue
Krantz, Bryan A.
Miao, Edward A.
Venue: Journal of Experimental Medicine
Publisher: Rockefeller University Press
Published: 2016-08-29
Volume: 213
Issue: 10
Pages: 2113-2128
ISSN: 0022-1007 (ISSN-L)
1540-9538
DOI: 10.1084/jem.20151613
PMC: PMC5030797
OpenAlex: W2511127858
Cited by: 403
References: 43
Citations by year: 2026: 21 · 2025: 38 · 2024: 40 · 2023: 57 · 2022: 56 · 2021: 35 · 2020: 46 · 2019: 35 · 2018: 37 · 2017: 32 · 2016: 5
FWCI: 18.89
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: The Journal of Experimental Medicine (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
PubMed Central (publishedVersion, cc-by-nc-sa)
PubMed (publishedVersion)
Carolina Digital Repository (University of North Carolina at Chapel Hill) (submittedVersion)
UNC Libraries
Funders: National Institutes of Health (DK007737, AI097518, AI057141, AI119073, AI077703, 1 S10 OD017984-01A1)
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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Keywords: pyroptosis, caspase-1, inflammasome, intracellular bacteria, bacterial clearance, efferocytosis, neutrophils, macrophages, osmotic lysis, plasma membrane rupture, necroptosis, neutrophil extracellular traps, complement system, scavenger receptors, Salmonella, innate immunity
MeSH terms: Pyroptosis, Animals, Complement System Proteins, Macrophages, Mice, Inbred C57BL, Necrosis, Neutrophils, Phagocytosis, Salmonella typhimurium, Solubility, Intracellular Space, Green Fluorescent Proteins, Microbial Viability, Receptors, Scavenger, Mice

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Pyroptosis triggers pore-induced intracellular traps (PITs) that capture bacteria and lead to their clearance by efferocytosis

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