STING promotes NLRP3 localization in ER and facilitates NLRP3 deubiquitination to activate the inflammasome upon HSV-1 infection

One of the fundamental reactions of the innate immune responses to pathogen infection is the release of pro-inflammatory cytokines, including IL-1β, processed by the NLRP3 inflammasome. The stimulator of interferon genes (STING) has the essential roles in innate immune response against pathogen infe...

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Published inPLoS pathogens Vol. 16; no. 3; p. e1008335
Main Authors Wang, Wenbiao, Hu, Dingwen, Wu, Caifeng, Feng, Yuqian, Li, Aixin, Liu, Weiyong, Wang, Yingchong, Chen, Keli, Tian, Mingfu, Xiao, Feng, Zhang, Qi, Shereen, Muhammad Adnan, Chen, Weijie, Pan, Pan, Wan, Pin, Wu, Kailang, Wu, Jianguo
Format Journal Article
LanguageEnglish
Published United States Public Library of Science 18.03.2020
Public Library of Science (PLoS)
Subjects
Activation
Biological response modifiers
Biology and Life Sciences
Cell lines
Cells (Biology)
Cytokines
Deoxyribonucleic acid
DNA
Endoplasmic reticulum
Genes
Health aspects
Herpes viruses
IL-1β
Immune response
Immune system
Infection
Infections
Inflammasomes
Inflammation
Innate immunity
Interferon
Laboratories
Life sciences
Localization
Medicine and Health Sciences
Pathogens
Plasmids
Proteins
Research and analysis methods
Stimulators
Virology
China
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Abstract One of the fundamental reactions of the innate immune responses to pathogen infection is the release of pro-inflammatory cytokines, including IL-1β, processed by the NLRP3 inflammasome. The stimulator of interferon genes (STING) has the essential roles in innate immune response against pathogen infections. Here we reveal a distinct mechanism by which STING regulates the NLRP3 inflammasome activation, IL-1β secretion, and inflammatory responses in human cell lines, mice primary cells, and mice. Interestingly, upon HSV-1 infection and cytosolic DNA stimulation, STING binds to NLRP3 and promotes the inflammasome activation through two approaches. First, STING recruits NLRP3 and facilitates NLRP3 localization in the endoplasmic reticulum, thereby facilitating the inflammasome formation. Second, STING interacts with NLRP3 and attenuates K48- and K63-linked polyubiquitination of NLRP3, thereby promoting the inflammasome activation. Collectively, we demonstrate that the cGAS-STING-NLRP3 signaling is essential for host defense against HSV-1 infection.
AbstractList One of the fundamental reactions of the innate immune responses to pathogen infection is the release of pro-inflammatory cytokines, including IL-1β, processed by the NLRP3 inflammasome. The stimulator of interferon genes (STING) has the essential roles in innate immune response against pathogen infections. Here we reveal a distinct mechanism by which STING regulates the NLRP3 inflammasome activation, IL-1β secretion, and inflammatory responses in human cell lines, mice primary cells, and mice. Interestingly, upon HSV-1 infection and cytosolic DNA stimulation, STING binds to NLRP3 and promotes the inflammasome activation through two approaches. First, STING recruits NLRP3 and facilitates NLRP3 localization in the endoplasmic reticulum, thereby facilitating the inflammasome formation. Second, STING interacts with NLRP3 and attenuates K48- and K63-linked polyubiquitination of NLRP3, thereby promoting the inflammasome activation. Collectively, we demonstrate that the cGAS-STING-NLRP3 signaling is essential for host defense against HSV-1 infection.
One of the fundamental reactions of the innate immune responses to pathogen infection is the release of pro-inflammatory cytokines, including IL-1β, processed by the NLRP3 inflammasome. The stimulator of interferon genes (STING) has the essential roles in innate immune response against pathogen infections. Here we reveal a distinct mechanism by which STING regulates the NLRP3 inflammasome activation, IL-1β secretion, and inflammatory responses in human cell lines, mice primary cells, and mice. Interestingly, upon HSV-1 infection and cytosolic DNA stimulation, STING binds to NLRP3 and promotes the inflammasome activation through two approaches. First, STING recruits NLRP3 and facilitates NLRP3 localization in the endoplasmic reticulum, thereby facilitating the inflammasome formation. Second, STING interacts with NLRP3 and attenuates K48- and K63-linked polyubiquitination of NLRP3, thereby promoting the inflammasome activation. Collectively, we demonstrate that the cGAS-STING-NLRP3 signaling is essential for host defense against HSV-1 infection. The innate immune system is a primary host defense strategy to suppress the pathogen infections. One of the fundamental reactions of the innate immunity is the release of pro-inflammatory cytokines, including interleukine-1β (IL-1β), regulated by inflammasomes. The best-characterized inflammasomes is the NLRP3 inflammasome. STING has the essential roles in innate immune response against pathogen infections and is required for pathogen-induced inflammasome activation and IL-1β secretion. This study explores how STING regulates the NLRP3 inflammasome and reveals a distinct mechanism underlying such regulation upon herpes simplex virus type 1 (HSV-1) infection and cytosolic DNA stimulation. The authors propose that the cGAS-STING-NLRP3 axis is essential for host defense against HSV-1 infection.
One of the fundamental reactions of the innate immune responses to pathogen infection is the release of pro-inflammatory cytokines, including IL-1[beta], processed by the NLRP3 inflammasome. The stimulator of interferon genes (STING) has the essential roles in innate immune response against pathogen infections. Here we reveal a distinct mechanism by which STING regulates the NLRP3 inflammasome activation, IL-1[beta] secretion, and inflammatory responses in human cell lines, mice primary cells, and mice. Interestingly, upon HSV-1 infection and cytosolic DNA stimulation, STING binds to NLRP3 and promotes the inflammasome activation through two approaches. First, STING recruits NLRP3 and facilitates NLRP3 localization in the endoplasmic reticulum, thereby facilitating the inflammasome formation. Second, STING interacts with NLRP3 and attenuates K48- and K63-linked polyubiquitination of NLRP3, thereby promoting the inflammasome activation. Collectively, we demonstrate that the cGAS-STING-NLRP3 signaling is essential for host defense against HSV-1 infection.
One of the fundamental reactions of the innate immune responses to pathogen infection is the release of pro-inflammatory cytokines, including IL-1β, processed by the NLRP3 inflammasome. The stimulator of interferon genes (STING) has the essential roles in innate immune response against pathogen infections. Here we reveal a distinct mechanism by which STING regulates the NLRP3 inflammasome activation, IL-1β secretion, and inflammatory responses in human cell lines, mice primary cells, and mice. Interestingly, upon HSV-1 infection and cytosolic DNA stimulation, STING binds to NLRP3 and promotes the inflammasome activation through two approaches. First, STING recruits NLRP3 and facilitates NLRP3 localization in the endoplasmic reticulum, thereby facilitating the inflammasome formation. Second, STING interacts with NLRP3 and attenuates K48- and K63-linked polyubiquitination of NLRP3, thereby promoting the inflammasome activation. Collectively, we demonstrate that the cGAS-STING-NLRP3 signaling is essential for host defense against HSV-1 infection.One of the fundamental reactions of the innate immune responses to pathogen infection is the release of pro-inflammatory cytokines, including IL-1β, processed by the NLRP3 inflammasome. The stimulator of interferon genes (STING) has the essential roles in innate immune response against pathogen infections. Here we reveal a distinct mechanism by which STING regulates the NLRP3 inflammasome activation, IL-1β secretion, and inflammatory responses in human cell lines, mice primary cells, and mice. Interestingly, upon HSV-1 infection and cytosolic DNA stimulation, STING binds to NLRP3 and promotes the inflammasome activation through two approaches. First, STING recruits NLRP3 and facilitates NLRP3 localization in the endoplasmic reticulum, thereby facilitating the inflammasome formation. Second, STING interacts with NLRP3 and attenuates K48- and K63-linked polyubiquitination of NLRP3, thereby promoting the inflammasome activation. Collectively, we demonstrate that the cGAS-STING-NLRP3 signaling is essential for host defense against HSV-1 infection.
Audience Academic
Author Wu, Caifeng
Zhang, Qi
Xiao, Feng
Liu, Weiyong
Pan, Pan
Feng, Yuqian
Wu, Kailang
Wan, Pin
Tian, Mingfu
Shereen, Muhammad Adnan
Chen, Weijie
Wu, Jianguo
Wang, Wenbiao
Li, Aixin
Wang, Yingchong
Chen, Keli
Hu, Dingwen
AuthorAffiliation 1 Guangdong Key Laboratory of Virology, Institute of Medical Microbiology, Jinan University, Guangzhou, China
Florida State University, UNITED STATES
2 State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, China
AuthorAffiliation_xml – name: 1 Guangdong Key Laboratory of Virology, Institute of Medical Microbiology, Jinan University, Guangzhou, China
– name: Florida State University, UNITED STATES
– name: 2 State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, China
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  orcidid: 0000-0002-8326-2895
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/32187211$$D View this record in MEDLINE/PubMed
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Snippet One of the fundamental reactions of the innate immune responses to pathogen infection is the release of pro-inflammatory cytokines, including IL-1β, processed...
One of the fundamental reactions of the innate immune responses to pathogen infection is the release of pro-inflammatory cytokines, including IL-1[beta],...
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StartPage e1008335
SubjectTerms Activation
Biological response modifiers
Biology and Life Sciences
Cell lines
Cells (Biology)
Cytokines
Deoxyribonucleic acid
DNA
Endoplasmic reticulum
Genes
Health aspects
Herpes viruses
IL-1β
Immune response
Immune system
Infection
Infections
Inflammasomes
Inflammation
Innate immunity
Interferon
Laboratories
Life sciences
Localization
Medicine and Health Sciences
Pathogens
Plasmids
Proteins
Research and analysis methods
Stimulators
Virology
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Title STING promotes NLRP3 localization in ER and facilitates NLRP3 deubiquitination to activate the inflammasome upon HSV-1 infection
URI https://www.ncbi.nlm.nih.gov/pubmed/32187211
https://www.proquest.com/docview/2390750154
https://www.proquest.com/docview/2379020896
https://pubmed.ncbi.nlm.nih.gov/PMC7080238
https://doaj.org/article/1f1ea353a43944d3ab8ede1e3144c959
http://dx.doi.org/10.1371/journal.ppat.1008335
Volume 16
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