Random mutagenesis of the nucleotide‐binding domain of NRC 1 ( NB ‐ LRR Required for Hypersensitive Response‐Associated Cell Death‐1), a downstream signalling nucleotide‐binding, leucine‐rich repeat ( NB ‐ LRR ) protein, identifies gain‐of‐function mutations in the nucleotide‐binding pocket

2015 ◽  
Vol 208 (1) ◽  
pp. 210-223 ◽  
Author(s):  
Daniela J. Sueldo ◽  
Mahdere Shimels ◽  
Laurentiu N. Spiridon ◽  
Octav Caldararu ◽  
Andrei‐Jose Petrescu ◽  
...  
Keyword(s):  
Cell Death ◽  
Hypersensitive Response ◽  
Random Mutagenesis ◽  
Nucleotide Binding ◽  
Binding Pocket ◽  
Binding Domain ◽  
Leucine Rich Repeat ◽  
Nucleotide Binding Domain ◽  
Gain Of Function ◽  
Lrr Protein

scholarly journals Osteoblasts Express NLRP3, a Nucleotide-Binding Domain and Leucine-Rich Repeat Region Containing Receptor Implicated in Bacterially Induced Cell Death

2007 ◽  
Vol 23 (1) ◽  
pp. 30-40 ◽  
Author(s):  
Samuel H McCall ◽  
Mahnaz Sahraei ◽  
Amy B Young ◽  
Charles S Worley ◽  
Joseph A Duncan ◽  
...  
Keyword(s):  
Cell Death ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Leucine Rich Repeat ◽  
Repeat Region ◽  
Nucleotide Binding Domain

scholarly journals Inflammasome Components Coordinate Autophagy and Pyroptosis as Macrophage Responses to Infection

mBio ◽  
2013 ◽  
Vol 4 (1) ◽  
Author(s):  
Brenda G. Byrne ◽  
Jean-Francois Dubuisson ◽  
Amrita D. Joshi ◽  
Jenny J. Persson ◽  
Michele S. Swanson
Keyword(s):  
Cell Death ◽  
Legionella Pneumophila ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Mouse Genetics ◽  
Leucine Rich Repeat ◽  
Nucleotide Binding Domain ◽  
Caspase 1 ◽  
Primary Mouse ◽  
Mouse Macrophages

ABSTRACTWhen microbes contaminate the macrophage cytoplasm, leukocytes undergo a proinflammatory death that is initiated by nucleotide-binding-domain-, leucine-rich-repeat-containing proteins (NLR proteins) that bind and activate caspase-1. We report that these inflammasome components also regulate autophagy, a vesicular pathway to eliminate cytosolic debris. In response to infection with flagellateLegionella pneumophila, C57BL/6J mouse macrophages equipped with caspase-1 and the NLR proteins NAIP5 and NLRC4 stimulated autophagosome turnover. A second trigger of inflammasome assembly, K+efflux, also rapidly activated autophagy in macrophages that produced caspase-1. Autophagy protects infected macrophages from pyroptosis, since caspase-1-dependent cell death occurred more frequently when autophagy was dampened pharmacologically by either 3-methyladenine or an inhibitor of the Atg4 protease. Accordingly, in addition to coordinating pyroptosis, both (pro-) caspase-1 protein and NLR components of inflammasomes equip macrophages to recruit autophagy, a disposal pathway that raises the threshold of contaminants necessary to trigger proinflammatory leukocyte death.IMPORTANCEAn exciting development in the innate-immunity field is the recognition that macrophages enlist autophagy to protect their cytoplasm from infection. Nutrient deprivation has long been known to induce autophagy; how infection triggers this disposal pathway is an active area of research. Autophagy is encountered by many of the intracellular pathogens that are known to trigger pyroptosis, an inflammatory cell death initiated when nucleotide-binding-domain-, leucine-rich-repeat-containing proteins (NLR proteins) activate caspase-1 within inflammasome complexes. Therefore, we tested the hypothesis that NLR proteins and caspase-1 also coordinate autophagy as a barrier to cytosolic infection. By exploiting classical bacterial and mouse genetics and kinetic assays of autophagy, we demonstrate for the first time that, when confronted with cytosolic contamination, primary mouse macrophages rely not only on the NLR proteins NAIP5 and NLRC4 but also on (pro-)caspase-1 protein to mount a rapid autophagic response that wards off proinflammatory cell death.

scholarly journals A Novel Aminosaccharide Compound Blocks Immune Responses by Toll-like Receptors and Nucleotide-binding Domain, Leucine-rich Repeat Proteins

2010 ◽  
Vol 286 (7) ◽  
pp. 5727-5735 ◽  
Author(s):  
Kyoung-Hee Lee ◽  
Yuen-Joyce Liu ◽  
Amlan Biswas ◽  
Chikako Ogawa ◽  
Koichi S. Kobayashi
Keyword(s):  
Immune Responses ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Leucine Rich Repeat ◽  
Toll Like Receptors ◽  
Nucleotide Binding Domain ◽  
Repeat Proteins

scholarly journals Broad detection of bacterial type III secretion system and flagellin proteins by the human NAIP/NLRC4 inflammasome

2017 ◽  
Vol 114 (50) ◽  
pp. 13242-13247 ◽  
Author(s):  
Valeria M. Reyes Ruiz ◽  
Jasmine Ramirez ◽  
Nawar Naseer ◽  
Nicole M. Palacio ◽  
Ingharan J. Siddarthan ◽  
...  
Keyword(s):  
Type Iii Secretion ◽  
Bacterial Species ◽  
Type Iii Secretion System ◽  
Nucleotide Binding ◽  
Secretion System ◽  
Binding Domain ◽  
Leucine Rich Repeat ◽  
Nucleotide Binding Domain ◽  
Type Iii ◽  
Needle Protein

Inflammasomes are cytosolic multiprotein complexes that initiate host defense against bacterial pathogens by activating caspase-1–dependent cytokine secretion and cell death. In mice, specific nucleotide-binding domain, leucine-rich repeat-containing family, apoptosis inhibitory proteins (NAIPs) activate the nucleotide-binding domain, leucine-rich repeat-containing family, CARD domain-containing protein 4 (NLRC4) inflammasome upon sensing components of the type III secretion system (T3SS) and flagellar apparatus. NAIP1 recognizes the T3SS needle protein, NAIP2 recognizes the T3SS inner rod protein, and NAIP5 and NAIP6 recognize flagellin. In contrast, humans encode a single functional NAIP, raising the question of whether human NAIP senses one or multiple bacterial ligands. Previous studies found that human NAIP detects both flagellin and the T3SS needle protein and suggested that the ability to detect both ligands was achieved by multiple isoforms encoded by the single humanNAIPgene. Here, we show that human NAIP also senses theSalmonellaTyphimurium T3SS inner rod protein PrgJ and that T3SS inner rod proteins from multiple bacterial species are also detected. Furthermore, we show that a single human NAIP isoform is capable of sensing the T3SS inner rod, needle, and flagellin. Our findings indicate that, in contrast to murine NAIPs, promiscuous recognition of multiple bacterial ligands is conferred by a single human NAIP.

NOD-like subfamily of the nucleotide-binding domain and leucine-rich repeat containing family receptors and their expression in channel catfish

2009 ◽  
Vol 33 (9) ◽  
pp. 991-999 ◽  
Author(s):  
Zhenxia Sha ◽  
Jason W. Abernathy ◽  
Shaolin Wang ◽  
Ping Li ◽  
Huseyin Kucuktas ◽  
...  
Keyword(s):  
Channel Catfish ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Leucine Rich Repeat ◽  
Nucleotide Binding Domain

NLRs: Nucleotide-Binding Domain and Leucine-Rich-Repeat-Containing Proteins

EcoSal ◽  
2009 ◽  
Author(s):  
Leticia A. M. Carneiro ◽  
Jörg H. Fritz ◽  
Thomas A. Kufer ◽  
Leonardo H. Travassos ◽  
Szilvia Benko ◽  
...  
Keyword(s):  
Nucleotide Binding ◽  
Binding Domain ◽  
Leucine Rich Repeat ◽  
Nucleotide Binding Domain
Sign in / Sign up

Export Citation Format

Share Document