Juruj, C. and Lelogeais, V. and Pierini, R. and Perret, M. and Py, B. F. and Jamilloux, Y. and Broz, P. and Ader, F. and Faure, M. and Henry, T.. (2013) Caspase-1 activity affects AIM2 speck formation/stability through a negative feedback loop. Frontiers in Cellular and Infection Microbiology, 3. p. 14.
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Official URL: http://edoc.unibas.ch/49022/
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Abstract
The inflammasome is an innate immune signaling platform leading to caspase-1 activation, maturation of pro-inflammatory cytokines and cell death. Recognition of DNA within the host cytosol induces the formation of a large complex composed of the AIM2 receptor, the ASC adaptor and the caspase-1 effector. Francisella tularensis, the agent of tularemia, replicates within the host cytosol. The macrophage cytosolic surveillance system detects Francisella through the AIM2 inflammasome. Upon Francisella novicida infection, we observed a faster kinetics of AIM2 speck formation in ASC(KO) and Casp1(KO) as compared to WT macrophages. This observation was validated by a biochemical approach thus demonstrating for the first time the existence of a negative feedback loop controlled by ASC/caspase-1 that regulates AIM2 complex formation/stability. This regulatory mechanism acted before pyroptosis and required caspase-1 catalytic activity. Our data suggest that sublytic caspase-1 activity could delay the formation of stable AIM2 speck, an inflammasome complex associated with cell death.
Faculties and Departments: | 05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Infection Biology (Broz) |
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UniBasel Contributors: | Broz, Petr |
Item Type: | Article, refereed |
Article Subtype: | Research Article |
Publisher: | Frontiers Media |
e-ISSN: | 2235-2988 |
Note: | Publication type according to Uni Basel Research Database: Journal article |
Identification Number: |
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Last Modified: | 03 Oct 2017 09:58 |
Deposited On: | 03 Oct 2017 09:58 |
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