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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
2010-4-22
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pubmed:abstractText |
Vibrio vulnificus and Vibrio cholerae are Gram-negative pathogens that cause serious infectious disease in humans. The beta form of pro-IL-1 is thought to be involved in inflammatory responses and disease development during infection with these pathogens, but the mechanism of beta form of pro-IL-1 production remains poorly defined. In this study, we demonstrate that infection of mouse macrophages with two pathogenic Vibrio triggers the activation of caspase-1 via the NLRP3 inflammasome. Activation of the NLRP3 inflammasome was mediated by hemolysins and multifunctional repeat-in-toxins produced by the pathogenic bacteria. NLRP3 activation in response to V. vulnificus infection required NF-kappaB activation, which was mediated via TLR signaling. V. cholerae-induced NLRP3 activation also required NF-kappaB activation but was independent of TLR stimulation. Studies with purified V. cholerae hemolysin revealed that toxin-stimulated NLRP3 activation was induced by TLR and nucleotide-binding oligomerization domain 1/2 ligand-mediated NF-kappaB activation. Our results identify the NLRP3 inflammasome as a sensor of Vibrio infections through the action of bacterial cytotoxins and differential activation of innate signaling pathways acting upstream of NF-kappaB.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/CIAS1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Card15 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Card4 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-1beta,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/Nod1 Signaling Adaptor Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Nod2 Signaling Adaptor Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Toll-Like Receptors
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1550-6606
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pubmed:author |
pubmed-author:AkiraShizuoS,
pubmed-author:FranchiLuigiL,
pubmed-author:HigaNaomiN,
pubmed-author:KoizumiYukikoY,
pubmed-author:McCoyAndrea JAJ,
pubmed-author:NúñezGabrielG,
pubmed-author:NakasoneNoboruN,
pubmed-author:OguraYasunoriY,
pubmed-author:SagaraJunjiJ,
pubmed-author:SuzukiToshihikoT,
pubmed-author:TaniguchiShun'ichiroS,
pubmed-author:TomaClaudiaC,
pubmed-author:TschoppJürgJ,
pubmed-author:TsutsuiHirokoH,
pubmed-author:UematsuSatoshiS
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
184
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5287-97
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pubmed:meshHeading |
pubmed-meshheading:20348425-Animals,
pubmed-meshheading:20348425-Bacterial Toxins,
pubmed-meshheading:20348425-Bone Marrow Cells,
pubmed-meshheading:20348425-Carrier Proteins,
pubmed-meshheading:20348425-Caspase 1,
pubmed-meshheading:20348425-Immunity, Innate,
pubmed-meshheading:20348425-Inflammation,
pubmed-meshheading:20348425-Interleukin-1beta,
pubmed-meshheading:20348425-Ligands,
pubmed-meshheading:20348425-Macrophages,
pubmed-meshheading:20348425-Mice,
pubmed-meshheading:20348425-Mice, Inbred C57BL,
pubmed-meshheading:20348425-Mice, Knockout,
pubmed-meshheading:20348425-NF-kappa B,
pubmed-meshheading:20348425-Nod1 Signaling Adaptor Protein,
pubmed-meshheading:20348425-Nod2 Signaling Adaptor Protein,
pubmed-meshheading:20348425-Signal Transduction,
pubmed-meshheading:20348425-Toll-Like Receptors,
pubmed-meshheading:20348425-Vibrio cholerae,
pubmed-meshheading:20348425-Vibrio vulnificus
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pubmed:year |
2010
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pubmed:articleTitle |
Pathogenic Vibrio activate NLRP3 inflammasome via cytotoxins and TLR/nucleotide-binding oligomerization domain-mediated NF-kappa B signaling.
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pubmed:affiliation |
Division of Bacterial Pathogenesis, Graduate School of Medicine, University of the Ryukyus, Okinawa.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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