Caspase-4 Activation and Recruitment to Intracellular Gram-Negative Bacteria

Details

Serval ID
serval:BIB_E522DEB8F2BC
Type
A part of a book
Publication sub-type
Chapter: chapter ou part
Collection
Publications
Institution
Title
Caspase-4 Activation and Recruitment to Intracellular Gram-Negative Bacteria
Title of the book
Methods in Molecular Biology
Author(s)
Dilucca Marisa, Broz Petr
Publisher
Springer US
ISBN
9781071630396
9781071630402
Publication state
Published
Issued date
2023
Peer-reviewed
Oui
Volume
2641
Pages
49-65
Language
english
Abstract
The non-canonical inflammasome pathway functions as the primary cytosolic innate immune detection mechanism for Gram-negative bacterial lipopolysaccharide (LPS) in human and mouse cells and controls the proteolytic activation of the cell death executor gasdermin D (GSDMD). The main effectors of this pathways are the inflammatory proteases caspase-11 in mice and caspase-4/caspase-5 in humans. These caspases have been shown to bind LPS directly; however, the interaction between LPS and caspase-4/caspase-11 requires a set of interferon (IFN)-inducible GTPases, known as guanylate-binding proteins (GBPs). These GBPs assemble to form coatomers on cytosolic Gram-negative bacteria, which function as recruitment and activation platforms for caspase-11/caspase-4. Here we describe an assay to monitor caspase-4 activation in human cells by immunoblotting and its recruitment to intracellular bacteria using the model pathogen Burkholderia thailandensis.
Keywords
Humans, Animals, Mice, Lipopolysaccharides/metabolism, GTP-Binding Proteins/metabolism, Gram-Negative Bacteria/metabolism, Caspases/metabolism, Inflammasomes/metabolism, Cell Death, Burkholderia thailandensis, Caspase-4, Guanylate-binding proteins, Inflammasome, Lipopolysaccharide
Pubmed
Create date
01/05/2023 10:08
Last modification date
21/10/2023 6:07
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