The Nucleotide-Binding Domain, Leucine-Rich Repeat Protein 3 Inflammasome/IL-1 Receptor I Axis Mediates Innate, but Not Adaptive, Immune Responses after Exposure to Particulate Matter under 10 μm

2015 ◽  
Vol 52 (1) ◽  
pp. 96-105 ◽  
Author(s):  
Jeremy A. Hirota ◽  
Matthew J. Gold ◽  
Paul R. Hiebert ◽  
Leigh G. Parkinson ◽  
Tracee Wee ◽  
...  
Keyword(s):  
Particulate Matter ◽  
Immune Responses ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Leucine Rich Repeat ◽  
Nucleotide Binding Domain ◽  
Adaptive Immune Responses ◽  
Repeat Protein ◽  
Adaptive Immune ◽  
Leucine Rich Repeat Protein

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 Importance of OsRac1 and RAI1 in signalling of nucleotide‐binding site leucine‐rich repeat protein‐mediated resistance to rice blast disease

2019 ◽  
Vol 223 (2) ◽  
pp. 828-838 ◽  
Author(s):  
Zhuangzhi Zhou ◽  
Zhiqian Pang ◽  
Shengli Zhao ◽  
Lingli Zhang ◽  
Qiming Lv ◽  
...  
Keyword(s):  
Binding Site ◽  
Rice Blast ◽  
Nucleotide Binding ◽  
Nucleotide Binding Site ◽  
Rice Blast Disease ◽  
Blast Disease ◽  
Leucine Rich Repeat ◽  
Repeat Protein ◽  
Leucine Rich Repeat Protein

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.

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