Molecular mechanisms of inflammasome activation during microbial infections.

Détails

ID Serval
serval:BIB_AE100B0296E4
Type
Article: article d'un périodique ou d'un magazine.
Sous-type
Synthèse (review): revue aussi complète que possible des connaissances sur un sujet, rédigée à partir de l'analyse exhaustive des travaux publiés.
Collection
Publications
Titre
Molecular mechanisms of inflammasome activation during microbial infections.
Périodique
Immunological Reviews
Auteur(s)
Broz P., Monack D.M.
ISSN
1600-065X (Electronic)
ISSN-L
0105-2896
Statut éditorial
Publié
Date de publication
2011
Peer-reviewed
Oui
Volume
243
Numéro
1
Pages
174-190
Langue
anglais
Résumé
The innate immune system plays a crucial role in the rapid recognition and elimination of invading microbes. Detection of microbes relies on germ-line encoded pattern recognition receptors (PRRs) that recognize essential bacterial molecules, so-called pathogen-associated molecular patterns (PAMPs). A subset of PRRs, belonging to the NOD-like receptor (NLR) and the PYHIN protein families, detects viral and bacterial pathogens in the cytosol of host cells and induces the assembly of a multi-protein signaling platform called the inflammasome. The inflammasome serves as an activation platform for the mammalian cysteine protease caspase-1, a central mediator of innate immunity. Active caspase-1 promotes the maturation and release of interleukin-1β (IL-1β) and IL-18 as well as protein involved in cytoprotection and tissue repair. In addition, caspase-1 initiates a novel form of cell death called pyroptosis. Here, we discuss latest advances and our insights on inflammasome stimulation by two model intracellular pathogens, Francisella tularensis and Salmonella typhimurium. Recent studies on these pathogens have significantly shaped our understanding of the molecular mechanisms of inflammasome activation and how microbes can evade or manipulate inflammasome activity. In addition, we review the role of the inflammasome adapter ASC in caspase-1 autoproteolysis and new insights into the structure of the inflammasome complex.

Mots-clé
Animals, Antigens, Bacterial/immunology, Bacterial Infections/immunology, CARD Signaling Adaptor Proteins, Caspase 1/metabolism, Cell Death/immunology, Cytoskeletal Proteins/immunology, Cytoskeletal Proteins/metabolism, Francisella tularensis/immunology, Francisella tularensis/pathogenicity, Humans, Immunity, Innate, Inflammasomes/immunology, Inflammasomes/metabolism, Interleukin-18/immunology, Interleukin-1beta/immunology, Receptors, Pattern Recognition/immunology, Salmonella typhimurium/immunology, Salmonella typhimurium/pathogenicity, Signal Transduction/immunology
Pubmed
Web of science
Création de la notice
25/10/2017 11:04
Dernière modification de la notice
20/08/2019 16:17
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