HIV-1 induces the first signal to activate the NLRP3 inflammasome in monocyte-derived macrophages
Background/Aims: Inflammasomes are multimolecular complexes that regulate caspase-1. They act as sensors for endogenous and exogenous signals, and mediate the processing of pro-IL-1ß into its secreted, biologically active form. The NLRP3 inflammasome and IL-1ß are particularly interesting because th...
- Autores:
-
Hernández López, Juan Carlos
Latz E.
Urcuqui-Inchima S.
- Tipo de recurso:
- Article of journal
- Fecha de publicación:
- 2013
- Institución:
- Universidad Cooperativa de Colombia
- Repositorio:
- Repositorio UCC
- Idioma:
- OAI Identifier:
- oai:repository.ucc.edu.co:20.500.12494/41805
- Palabra clave:
- cryopyrin
immunoglobulin enhancer binding protein
inflammasome
interleukin 1beta
immunoglobulin enhancer binding protein
interleukin 1beta
article
controlled study
cytokine release
enzyme linked immunosorbent assay
human
human cell
Human immunodeficiency virus 1 infection
macrophage
priority journal
protein induction
signal transduction
virus envelope
Article
envelope gene
Human immunodeficiency virus 1
Human immunodeficiency virus 1 infection
macrophage
monocyte
nonhuman
Carrier Proteins
Cells
Cultured
Enzyme-Linked Immunosorbent Assay
HIV-1
Humans
Inflammasomes
Interleukin-1beta
Macrophages
Human immunodeficiency virus 1
- Rights
- closedAccess
- License
- http://purl.org/coar/access_right/c_14cb
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Hernández López, Juan Carlos Latz E.Urcuqui-Inchima S.2021-12-16T22:15:48Z2021-12-16T22:15:48Z2013https://doi.org/10.16925/di.v18i23.129203005526https://hdl.handle.net/20.500.12494/41805Hernandez JC,Latz E,Urcuqui S. HIV-1 induces the first signal to activate the NLRP3 inflammasome in monocyte-derived macrophages. Intervirology. 2013. 57. (1):p. 36-42. .Background/Aims: Inflammasomes are multimolecular complexes that regulate caspase-1. They act as sensors for endogenous and exogenous signals, and mediate the processing of pro-IL-1ß into its secreted, biologically active form. The NLRP3 inflammasome and IL-1ß are particularly interesting because they are required for efficient control of viral infections. Indeed, HIV-1 induces expression of NLRP3 and IL-1ß in healthy controls, but not in HIV-1-infected patients. Here we evaluate whether HIV-1 can induce activation of the NLRP3 inflammasome. Methods: Human primary monocyte-derived macrophages were infected with HIV-1 in the absence or presence of classical NLRP3 inflammasome activators, and IL-1ß release was assessed by ELISA. Results: HIV-1 initiates the priming signal for NLRP3 inflammasome activation through the NF-?B-associated pathway in human primary monocyte-derived macrophages. Furthermore, priming of NLRP3 activation in response to HIV-1 was independent of the viral envelope, since similar results were observed with HIV-1 and pseudotyped HIV-1 lacking the env gene. Conclusion: Our findings suggest that HIV-1 infection promotes IL-1ß secretion by inducing the first signal for NLRP3 inflammasome activation, a phenomenon that may contribute to AIDS progression. Copyright © 2013 S. Karger AG, Basel.0000-0002-9200-5698juanc.hernandezl@campusucc.edu.co42-36S. Karger AGcryopyrinimmunoglobulin enhancer binding proteininflammasomeinterleukin 1betaimmunoglobulin enhancer binding proteininterleukin 1betaarticlecontrolled studycytokine releaseenzyme linked immunosorbent assayhumanhuman cellHuman immunodeficiency virus 1 infectionmacrophagepriority journalprotein inductionsignal transductionvirus envelopeArticleenvelope geneHuman immunodeficiency virus 1Human immunodeficiency virus 1 infectionmacrophagemonocytenonhumanCarrier ProteinsCellsCulturedEnzyme-Linked Immunosorbent AssayHIV-1HumansInflammasomesInterleukin-1betaMacrophagesHuman immunodeficiency virus 1HIV-1 induces the first signal to activate the NLRP3 inflammasome in monocyte-derived macrophagesArtículohttp://purl.org/coar/resource_type/c_6501http://purl.org/coar/resource_type/c_2df8fbb1http://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articlehttp://purl.org/redcol/resource_type/ARTinfo:eu-repo/semantics/publishedVersionIntervirologyinfo:eu-repo/semantics/closedAccesshttp://purl.org/coar/access_right/c_14cbPublication20.500.12494/41805oai:repository.ucc.edu.co:20.500.12494/418052024-08-20 16:21:13.441metadata.onlyhttps://repository.ucc.edu.coRepositorio Institucional Universidad Cooperativa de Colombiabdigital@metabiblioteca.com |
dc.title.spa.fl_str_mv |
HIV-1 induces the first signal to activate the NLRP3 inflammasome in monocyte-derived macrophages |
title |
HIV-1 induces the first signal to activate the NLRP3 inflammasome in monocyte-derived macrophages |
spellingShingle |
HIV-1 induces the first signal to activate the NLRP3 inflammasome in monocyte-derived macrophages cryopyrin immunoglobulin enhancer binding protein inflammasome interleukin 1beta immunoglobulin enhancer binding protein interleukin 1beta article controlled study cytokine release enzyme linked immunosorbent assay human human cell Human immunodeficiency virus 1 infection macrophage priority journal protein induction signal transduction virus envelope Article envelope gene Human immunodeficiency virus 1 Human immunodeficiency virus 1 infection macrophage monocyte nonhuman Carrier Proteins Cells Cultured Enzyme-Linked Immunosorbent Assay HIV-1 Humans Inflammasomes Interleukin-1beta Macrophages Human immunodeficiency virus 1 |
title_short |
HIV-1 induces the first signal to activate the NLRP3 inflammasome in monocyte-derived macrophages |
title_full |
HIV-1 induces the first signal to activate the NLRP3 inflammasome in monocyte-derived macrophages |
title_fullStr |
HIV-1 induces the first signal to activate the NLRP3 inflammasome in monocyte-derived macrophages |
title_full_unstemmed |
HIV-1 induces the first signal to activate the NLRP3 inflammasome in monocyte-derived macrophages |
title_sort |
HIV-1 induces the first signal to activate the NLRP3 inflammasome in monocyte-derived macrophages |
dc.creator.fl_str_mv |
Hernández López, Juan Carlos Latz E. Urcuqui-Inchima S. |
dc.contributor.author.none.fl_str_mv |
Hernández López, Juan Carlos Latz E. Urcuqui-Inchima S. |
dc.subject.spa.fl_str_mv |
cryopyrin immunoglobulin enhancer binding protein inflammasome interleukin 1beta immunoglobulin enhancer binding protein interleukin 1beta article controlled study cytokine release enzyme linked immunosorbent assay human human cell Human immunodeficiency virus 1 infection macrophage priority journal protein induction signal transduction virus envelope Article envelope gene Human immunodeficiency virus 1 Human immunodeficiency virus 1 infection macrophage monocyte nonhuman Carrier Proteins Cells Cultured Enzyme-Linked Immunosorbent Assay HIV-1 Humans Inflammasomes Interleukin-1beta Macrophages Human immunodeficiency virus 1 |
topic |
cryopyrin immunoglobulin enhancer binding protein inflammasome interleukin 1beta immunoglobulin enhancer binding protein interleukin 1beta article controlled study cytokine release enzyme linked immunosorbent assay human human cell Human immunodeficiency virus 1 infection macrophage priority journal protein induction signal transduction virus envelope Article envelope gene Human immunodeficiency virus 1 Human immunodeficiency virus 1 infection macrophage monocyte nonhuman Carrier Proteins Cells Cultured Enzyme-Linked Immunosorbent Assay HIV-1 Humans Inflammasomes Interleukin-1beta Macrophages Human immunodeficiency virus 1 |
description |
Background/Aims: Inflammasomes are multimolecular complexes that regulate caspase-1. They act as sensors for endogenous and exogenous signals, and mediate the processing of pro-IL-1ß into its secreted, biologically active form. The NLRP3 inflammasome and IL-1ß are particularly interesting because they are required for efficient control of viral infections. Indeed, HIV-1 induces expression of NLRP3 and IL-1ß in healthy controls, but not in HIV-1-infected patients. Here we evaluate whether HIV-1 can induce activation of the NLRP3 inflammasome. Methods: Human primary monocyte-derived macrophages were infected with HIV-1 in the absence or presence of classical NLRP3 inflammasome activators, and IL-1ß release was assessed by ELISA. Results: HIV-1 initiates the priming signal for NLRP3 inflammasome activation through the NF-?B-associated pathway in human primary monocyte-derived macrophages. Furthermore, priming of NLRP3 activation in response to HIV-1 was independent of the viral envelope, since similar results were observed with HIV-1 and pseudotyped HIV-1 lacking the env gene. Conclusion: Our findings suggest that HIV-1 infection promotes IL-1ß secretion by inducing the first signal for NLRP3 inflammasome activation, a phenomenon that may contribute to AIDS progression. Copyright © 2013 S. Karger AG, Basel. |
publishDate |
2013 |
dc.date.issued.none.fl_str_mv |
2013 |
dc.date.accessioned.none.fl_str_mv |
2021-12-16T22:15:48Z |
dc.date.available.none.fl_str_mv |
2021-12-16T22:15:48Z |
dc.type.none.fl_str_mv |
Artículo |
dc.type.coar.fl_str_mv |
http://purl.org/coar/resource_type/c_2df8fbb1 |
dc.type.coar.none.fl_str_mv |
http://purl.org/coar/resource_type/c_6501 |
dc.type.coarversion.none.fl_str_mv |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
dc.type.driver.none.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.redcol.none.fl_str_mv |
http://purl.org/redcol/resource_type/ART |
dc.type.version.none.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
http://purl.org/coar/resource_type/c_6501 |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
https://doi.org/10.16925/di.v18i23.1292 |
dc.identifier.issn.spa.fl_str_mv |
03005526 |
dc.identifier.uri.none.fl_str_mv |
https://hdl.handle.net/20.500.12494/41805 |
dc.identifier.bibliographicCitation.spa.fl_str_mv |
Hernandez JC,Latz E,Urcuqui S. HIV-1 induces the first signal to activate the NLRP3 inflammasome in monocyte-derived macrophages. Intervirology. 2013. 57. (1):p. 36-42. . |
url |
https://doi.org/10.16925/di.v18i23.1292 https://hdl.handle.net/20.500.12494/41805 |
identifier_str_mv |
03005526 Hernandez JC,Latz E,Urcuqui S. HIV-1 induces the first signal to activate the NLRP3 inflammasome in monocyte-derived macrophages. Intervirology. 2013. 57. (1):p. 36-42. . |
dc.relation.ispartofjournal.spa.fl_str_mv |
Intervirology |
dc.rights.accessrights.none.fl_str_mv |
info:eu-repo/semantics/closedAccess |
dc.rights.coar.none.fl_str_mv |
http://purl.org/coar/access_right/c_14cb |
eu_rights_str_mv |
closedAccess |
rights_invalid_str_mv |
http://purl.org/coar/access_right/c_14cb |
dc.format.extent.spa.fl_str_mv |
42-36 |
dc.publisher.spa.fl_str_mv |
S. Karger AG |
institution |
Universidad Cooperativa de Colombia |
repository.name.fl_str_mv |
Repositorio Institucional Universidad Cooperativa de Colombia |
repository.mail.fl_str_mv |
bdigital@metabiblioteca.com |
_version_ |
1814247122442125312 |