Irgm2 and Gate‐16 cooperatively dampen Gram‐negative bacteria‐induced caspase‐11 response

Inflammatory caspase‐11 (rodent) and caspases‐4/5 (humans) detect the Gram‐negative bacterial component LPS within the host cell cytosol, promoting activation of the non‐canonical inflammasome. Although non‐canonical inflammasome‐induced pyroptosis and IL‐1‐related cytokine release are crucial to mo...

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Published inEMBO reports Vol. 21; no. 11; pp. e50829 - n/a
Main Authors Eren, Elif, Planès, Rémi, Bagayoko, Salimata, Bordignon, Pierre‐Jean, Chaoui, Karima, Hessel, Audrey, Santoni, Karin, Pinilla, Miriam, Lagrange, Brice, Burlet‐Schiltz, Odile, Howard, Jonathan C, Henry, Thomas, Yamamoto, Masahiro, Meunier, Etienne
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 05.11.2020
Springer Nature B.V
EMBO Press
John Wiley and Sons Inc
Subjects
Animal biology
Autophagy
Autophagy-Related Protein 8 Family
Bacteria
Caspase
Caspases - genetics
Caspases, Initiator
Caspase‐11
Cell activation
Cytokines
Cytosol
EMBO07
EMBO19
EMBO23
Endotoxemia
Gate‐16
Gram-Negative Bacteria
Immune response
Immune system
infections/Interferons
Inflammasomes
Inflammasomes - genetics
Inflammation
Interferon
Intracellular
Irgm2
Life Sciences
Lipopolysaccharides
Macrophages
non‐canonical inflammasome
Phagocytosis
Proteins
Pyroptosis
Sepsis
Caspase‐11
infections/Interferons
Irgm2
Gate‐16
non‐canonical inflammasome
non-canonical inflammasome
Caspase-11
Gate-16
Virology & Host Pathogen Interaction
Immunology
Microbiology
non-canonical inflammasome Subject Categories Autophagy & Cell Death
Online AccessGet full text
ISSN1469-221X
1469-3178
1469-3178
DOI10.15252/embr.202050829

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Abstract Inflammatory caspase‐11 (rodent) and caspases‐4/5 (humans) detect the Gram‐negative bacterial component LPS within the host cell cytosol, promoting activation of the non‐canonical inflammasome. Although non‐canonical inflammasome‐induced pyroptosis and IL‐1‐related cytokine release are crucial to mount an efficient immune response against various bacteria, their unrestrained activation drives sepsis. This suggests that cellular components tightly control the threshold level of the non‐canonical inflammasome in order to ensure efficient but non‐deleterious inflammatory responses. Here, we show that the IFN‐inducible protein Irgm2 and the ATG8 family member Gate‐16 cooperatively counteract Gram‐negative bacteria‐induced non‐canonical inflammasome activation, both in cultured macrophages and in vivo . Specifically, the Irgm2/Gate‐16 axis dampens caspase‐11 targeting to intracellular bacteria, which lowers caspase‐11‐mediated pyroptosis and cytokine release. Deficiency in Irgm2 or Gate16 induces both guanylate binding protein (GBP)‐dependent and GBP‐independent routes for caspase‐11 targeting to intracellular bacteria. Our findings identify molecular effectors that fine‐tune bacteria‐activated non‐canonical inflammasome responses and shed light on the understanding of the immune pathways they control. Synopsis Caspase‐11 targets cytosolic Gram‐negative bacteria, inducing pyroptosis and IL‐1 maturation. IFN‐inducible GTPases promote caspase‐11 targeting to bacterial membranes, whereas Irgm2 and the non‐canonical autophagy protein Gate‐16 restrain unnecessary caspase‐11 targeting. Irgm2 and Gate16 cooperatively inhibit Gram‐negative bacteria‐induced non canonical inflammasome activation. Irgm2/Gate16 deficiency drives exaggerated caspase‐11 response in a GBP‐dependent and ‐independent manner. Irgm2 deficiency enhances endotoxemia susceptibility of mice. Graphical Abstract Caspase‐11 targets cytosolic Gram‐negative bacteria, inducing pyroptosis and IL‐1 maturation. IFN‐inducible GTPases promote caspase‐11 targeting to bacterial membranes, whereas Irgm2 and the non‐canonical autophagy protein Gate‐16 restrain unnecessary caspase‐11 targeting.
AbstractList Inflammatory caspase-11 (rodent) and caspases-4/5 (humans) detect the Gram-negative bacterial component LPS within the host cell cytosol, promoting activation of the non-canonical inflammasome. Although non-canonical inflammasome-induced pyroptosis and IL-1-related cytokine release are crucial to mount an efficient immune response against various bacteria, their unrestrained activation drives sepsis. This suggests that cellular components tightly control the threshold level of the non-canonical inflammasome in order to ensure efficient but non-deleterious inflammatory responses. Here, we show that the IFN-inducible protein Irgm2 and the ATG8 family member Gate-16 cooperatively counteract Gramnegative bacteria-induced non-canonical inflammasome activation, both in cultured macrophages and in vivo. Specifically, the Irgm2/Gate-16 axis dampens caspase-11 targeting to intracellular bacteria, which lowers caspase-11-mediated pyroptosis and cytokine release. Deficiency in Irgm2 or Gate16 induces both guanylate binding protein (GBP)-dependent and GBP-independent routes for caspase-11 targeting to intracellular bacteria. Our findings identify molecular effectors that fine-tune bacteria-activated noncanonical inflammasome responses and shed light on the understanding of the immune pathways they control.
Inflammatory caspase‐11 (rodent) and caspases‐4/5 (humans) detect the Gram‐negative bacterial component LPS within the host cell cytosol, promoting activation of the non‐canonical inflammasome. Although non‐canonical inflammasome‐induced pyroptosis and IL ‐1‐related cytokine release are crucial to mount an efficient immune response against various bacteria, their unrestrained activation drives sepsis. This suggests that cellular components tightly control the threshold level of the non‐canonical inflammasome in order to ensure efficient but non‐deleterious inflammatory responses. Here, we show that the IFN ‐inducible protein Irgm2 and the ATG 8 family member Gate‐16 cooperatively counteract Gram‐negative bacteria‐induced non‐canonical inflammasome activation, both in cultured macrophages and in vivo . Specifically, the Irgm2/Gate‐16 axis dampens caspase‐11 targeting to intracellular bacteria, which lowers caspase‐11‐mediated pyroptosis and cytokine release. Deficiency in Irgm2 or Gate16 induces both guanylate binding protein ( GBP )‐dependent and GBP ‐independent routes for caspase‐11 targeting to intracellular bacteria. Our findings identify molecular effectors that fine‐tune bacteria‐activated non‐canonical inflammasome responses and shed light on the understanding of the immune pathways they control. Caspase‐11 targets cytosolic Gram‐negative bacteria, inducing pyroptosis and IL ‐1 maturation. IFN ‐inducible GTP ases promote caspase‐11 targeting to bacterial membranes, whereas Irgm2 and the non‐canonical autophagy protein Gate‐16 restrain unnecessary caspase‐11 targeting.
Inflammatory caspase‐11 (rodent) and caspases‐4/5 (humans) detect the Gram‐negative bacterial component LPS within the host cell cytosol, promoting activation of the non‐canonical inflammasome. Although non‐canonical inflammasome‐induced pyroptosis and IL‐1‐related cytokine release are crucial to mount an efficient immune response against various bacteria, their unrestrained activation drives sepsis. This suggests that cellular components tightly control the threshold level of the non‐canonical inflammasome in order to ensure efficient but non‐deleterious inflammatory responses. Here, we show that the IFN‐inducible protein Irgm2 and the ATG8 family member Gate‐16 cooperatively counteract Gram‐negative bacteria‐induced non‐canonical inflammasome activation, both in cultured macrophages and in vivo . Specifically, the Irgm2/Gate‐16 axis dampens caspase‐11 targeting to intracellular bacteria, which lowers caspase‐11‐mediated pyroptosis and cytokine release. Deficiency in Irgm2 or Gate16 induces both guanylate binding protein (GBP)‐dependent and GBP‐independent routes for caspase‐11 targeting to intracellular bacteria. Our findings identify molecular effectors that fine‐tune bacteria‐activated non‐canonical inflammasome responses and shed light on the understanding of the immune pathways they control. Synopsis Caspase‐11 targets cytosolic Gram‐negative bacteria, inducing pyroptosis and IL‐1 maturation. IFN‐inducible GTPases promote caspase‐11 targeting to bacterial membranes, whereas Irgm2 and the non‐canonical autophagy protein Gate‐16 restrain unnecessary caspase‐11 targeting. Irgm2 and Gate16 cooperatively inhibit Gram‐negative bacteria‐induced non canonical inflammasome activation. Irgm2/Gate16 deficiency drives exaggerated caspase‐11 response in a GBP‐dependent and ‐independent manner. Irgm2 deficiency enhances endotoxemia susceptibility of mice. Graphical Abstract Caspase‐11 targets cytosolic Gram‐negative bacteria, inducing pyroptosis and IL‐1 maturation. IFN‐inducible GTPases promote caspase‐11 targeting to bacterial membranes, whereas Irgm2 and the non‐canonical autophagy protein Gate‐16 restrain unnecessary caspase‐11 targeting.
Inflammatory caspase‐11 (rodent) and caspases‐4/5 (humans) detect the Gram‐negative bacterial component LPS within the host cell cytosol, promoting activation of the non‐canonical inflammasome. Although non‐canonical inflammasome‐induced pyroptosis and IL‐1‐related cytokine release are crucial to mount an efficient immune response against various bacteria, their unrestrained activation drives sepsis. This suggests that cellular components tightly control the threshold level of the non‐canonical inflammasome in order to ensure efficient but non‐deleterious inflammatory responses. Here, we show that the IFN‐inducible protein Irgm2 and the ATG8 family member Gate‐16 cooperatively counteract Gram‐negative bacteria‐induced non‐canonical inflammasome activation, both in cultured macrophages and in vivo. Specifically, the Irgm2/Gate‐16 axis dampens caspase‐11 targeting to intracellular bacteria, which lowers caspase‐11‐mediated pyroptosis and cytokine release. Deficiency in Irgm2 or Gate16 induces both guanylate binding protein (GBP)‐dependent and GBP‐independent routes for caspase‐11 targeting to intracellular bacteria. Our findings identify molecular effectors that fine‐tune bacteria‐activated non‐canonical inflammasome responses and shed light on the understanding of the immune pathways they control. Synopsis Caspase‐11 targets cytosolic Gram‐negative bacteria, inducing pyroptosis and IL‐1 maturation. IFN‐inducible GTPases promote caspase‐11 targeting to bacterial membranes, whereas Irgm2 and the non‐canonical autophagy protein Gate‐16 restrain unnecessary caspase‐11 targeting. Irgm2 and Gate16 cooperatively inhibit Gram‐negative bacteria‐induced non canonical inflammasome activation. Irgm2/Gate16 deficiency drives exaggerated caspase‐11 response in a GBP‐dependent and ‐independent manner. Irgm2 deficiency enhances endotoxemia susceptibility of mice. Caspase‐11 targets cytosolic Gram‐negative bacteria, inducing pyroptosis and IL‐1 maturation. IFN‐inducible GTPases promote caspase‐11 targeting to bacterial membranes, whereas Irgm2 and the non‐canonical autophagy protein Gate‐16 restrain unnecessary caspase‐11 targeting.
Inflammatory caspase-11 (rodent) and caspases-4/5 (humans) detect the Gram-negative bacterial component LPS within the host cell cytosol, promoting activation of the non-canonical inflammasome. Although non-canonical inflammasome-induced pyroptosis and IL-1-related cytokine release are crucial to mount an efficient immune response against various bacteria, their unrestrained activation drives sepsis. This suggests that cellular components tightly control the threshold level of the non-canonical inflammasome in order to ensure efficient but non-deleterious inflammatory responses. Here, we show that the IFN-inducible protein Irgm2 and the ATG8 family member Gate-16 cooperatively counteract Gram-negative bacteria-induced non-canonical inflammasome activation, both in cultured macrophages and in vivo. Specifically, the Irgm2/Gate-16 axis dampens caspase-11 targeting to intracellular bacteria, which lowers caspase-11-mediated pyroptosis and cytokine release. Deficiency in Irgm2 or Gate16 induces both guanylate binding protein (GBP)-dependent and GBP-independent routes for caspase-11 targeting to intracellular bacteria. Our findings identify molecular effectors that fine-tune bacteria-activated non-canonical inflammasome responses and shed light on the understanding of the immune pathways they control.Inflammatory caspase-11 (rodent) and caspases-4/5 (humans) detect the Gram-negative bacterial component LPS within the host cell cytosol, promoting activation of the non-canonical inflammasome. Although non-canonical inflammasome-induced pyroptosis and IL-1-related cytokine release are crucial to mount an efficient immune response against various bacteria, their unrestrained activation drives sepsis. This suggests that cellular components tightly control the threshold level of the non-canonical inflammasome in order to ensure efficient but non-deleterious inflammatory responses. Here, we show that the IFN-inducible protein Irgm2 and the ATG8 family member Gate-16 cooperatively counteract Gram-negative bacteria-induced non-canonical inflammasome activation, both in cultured macrophages and in vivo. Specifically, the Irgm2/Gate-16 axis dampens caspase-11 targeting to intracellular bacteria, which lowers caspase-11-mediated pyroptosis and cytokine release. Deficiency in Irgm2 or Gate16 induces both guanylate binding protein (GBP)-dependent and GBP-independent routes for caspase-11 targeting to intracellular bacteria. Our findings identify molecular effectors that fine-tune bacteria-activated non-canonical inflammasome responses and shed light on the understanding of the immune pathways they control.
Inflammatory caspase‐11 (rodent) and caspases‐4/5 (humans) detect the Gram‐negative bacterial component LPS within the host cell cytosol, promoting activation of the non‐canonical inflammasome. Although non‐canonical inflammasome‐induced pyroptosis and IL‐1‐related cytokine release are crucial to mount an efficient immune response against various bacteria, their unrestrained activation drives sepsis. This suggests that cellular components tightly control the threshold level of the non‐canonical inflammasome in order to ensure efficient but non‐deleterious inflammatory responses. Here, we show that the IFN‐inducible protein Irgm2 and the ATG8 family member Gate‐16 cooperatively counteract Gram‐negative bacteria‐induced non‐canonical inflammasome activation, both in cultured macrophages and in vivo. Specifically, the Irgm2/Gate‐16 axis dampens caspase‐11 targeting to intracellular bacteria, which lowers caspase‐11‐mediated pyroptosis and cytokine release. Deficiency in Irgm2 or Gate16 induces both guanylate binding protein (GBP)‐dependent and GBP‐independent routes for caspase‐11 targeting to intracellular bacteria. Our findings identify molecular effectors that fine‐tune bacteria‐activated non‐canonical inflammasome responses and shed light on the understanding of the immune pathways they control.
Inflammatory caspase-11 (rodent) and caspases-4/5 (humans) detect the Gram-negative bacterial component LPS within the host cell cytosol, promoting activation of the non-canonical inflammasome. Although non-canonical inflammasome-induced pyroptosis and IL-1-related cytokine release are crucial to mount an efficient immune response against various bacteria, their unrestrained activation drives sepsis. This suggests that cellular components tightly control the threshold level of the non-canonical inflammasome in order to ensure efficient but non-deleterious inflammatory responses. Here, we show that the IFN-inducible protein Irgm2 and the ATG8 family member Gate-16 cooperatively counteract Gram-negative bacteria-induced non-canonical inflammasome activation, both in cultured macrophages and in vivo. Specifically, the Irgm2/Gate-16 axis dampens caspase-11 targeting to intracellular bacteria, which lowers caspase-11-mediated pyroptosis and cytokine release. Deficiency in Irgm2 or Gate16 induces both guanylate binding protein (GBP)-dependent and GBP-independent routes for caspase-11 targeting to intracellular bacteria. Our findings identify molecular effectors that fine-tune bacteria-activated non-canonical inflammasome responses and shed light on the understanding of the immune pathways they control.
Author Planès, Rémi
Lagrange, Brice
Meunier, Etienne
Eren, Elif
Santoni, Karin
Yamamoto, Masahiro
Burlet‐Schiltz, Odile
Henry, Thomas
Hessel, Audrey
Pinilla, Miriam
Chaoui, Karima
Bordignon, Pierre‐Jean
Howard, Jonathan C
Bagayoko, Salimata
AuthorAffiliation 5 Department of Immunoparasitology Research Institute for Microbial Diseases Osaka University Osaka Japan
4 Fundação Calouste Gulbenkian Instituto Gulbenkian de Ciência Oeiras Portugal
3 CIRI, Centre International de Recherche en Infectiologie Inserm, U1111 CNRS, UMR5308 École Normale Supérieure de Lyon Université Claude Bernard Lyon 1 Univ Lyon Lyon France
7 Present address: Institute of Pharmacology and Structural Biology (IPBS) CNRS Toulouse France
1 Institute of Pharmacology and Structural Biology (IPBS) CNRS, UMR5089 University of Toulouse Toulouse France
2 Mass Spectrometry Core Facility Institute of Pharmacology and Structural Biology (IPBS) CNRS, UMR5089 University of Toulouse Toulouse France
6 Laboratory of Immunoparasitology WPI Immunology Frontier Research Center Osaka University Osaka Japan
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  organization: Institute of Pharmacology and Structural Biology (IPBS), CNRS, UMR5089, University of Toulouse, Institute of Pharmacology and Structural Biology (IPBS), CNRS
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Issue 11
Keywords Caspase‐11
infections/Interferons
Irgm2
Gate‐16
non‐canonical inflammasome
non-canonical inflammasome
Caspase-11
Gate-16
Virology & Host Pathogen Interaction
Immunology
Microbiology
non-canonical inflammasome Subject Categories Autophagy & Cell Death
Language English
License 2020 The Authors.
Distributed under a Creative Commons Attribution 4.0 International License: http://creativecommons.org/licenses/by/4.0
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content type line 14
content type line 23
See also: R Finethy et al and A Linder & V Hornung (November 2020)
These authors contributed equally to this work
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33135287 - EMBO Rep. 2020 Nov 5;21(11):e51787
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Snippet Inflammatory caspase‐11 (rodent) and caspases‐4/5 (humans) detect the Gram‐negative bacterial component LPS within the host cell cytosol, promoting activation...
Inflammatory caspase-11 (rodent) and caspases-4/5 (humans) detect the Gram-negative bacterial component LPS within the host cell cytosol, promoting activation...
Inflammatory caspase‐11 (rodent) and caspases‐4/5 (humans) detect the Gram‐negative bacterial component LPS within the host cell cytosol, promoting activation...
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StartPage e50829
SubjectTerms Animal biology
Autophagy
Autophagy-Related Protein 8 Family
Bacteria
Caspase
Caspases - genetics
Caspases, Initiator
Caspase‐11
Cell activation
Cytokines
Cytosol
EMBO07
EMBO19
EMBO23
Endotoxemia
Gate‐16
Gram-Negative Bacteria
Immune response
Immune system
infections/Interferons
Inflammasomes
Inflammasomes - genetics
Inflammation
Interferon
Intracellular
Irgm2
Life Sciences
Lipopolysaccharides
Macrophages
non‐canonical inflammasome
Phagocytosis
Proteins
Pyroptosis
Sepsis
Title Irgm2 and Gate‐16 cooperatively dampen Gram‐negative bacteria‐induced caspase‐11 response
URI https://link.springer.com/article/10.15252/embr.202050829
https://onlinelibrary.wiley.com/doi/abs/10.15252%2Fembr.202050829
https://www.ncbi.nlm.nih.gov/pubmed/33124769
https://www.proquest.com/docview/2457846868
https://www.proquest.com/docview/2456416153
https://hal.science/hal-02997566
https://pubmed.ncbi.nlm.nih.gov/PMC7645206
Volume 21
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