Conserved nutrient sensor O-GlcNAc transferase is integral to C. elegans pathogen-specific immunity.
PLoS One
; 9(12): e113231, 2014.
Article
em En
| MEDLINE
| ID: mdl-25474640
ABSTRACT
Discriminating pathogenic bacteria from bacteria used as a food source is key to Caenorhabidits elegans immunity. Using mutants defective in the enzymes of O-linked N-acetylglucosamine (O-GlcNAc) cycling, we examined the role of this nutrient-sensing pathway in the C. elegans innate immune response. Genetic analysis showed that deletion of O-GlcNAc transferase (ogt-1) yielded animals hypersensitive to the human pathogen S. aureus but not to P. aeruginosa. Genetic interaction studies revealed that nutrient-responsive OGT-1 acts through the conserved ß-catenin (BAR-1) pathway and in concert with p38 MAPK (PMK-1) to modulate the immune response to S. aureus. Moreover, whole genome transcriptional profiling revealed that O-GlcNAc cycling mutants exhibited deregulation of unique stress- and immune-responsive genes. The participation of nutrient sensor OGT-1 in an immunity module evolutionarily conserved from C. elegans to humans reveals an unexplored nexus between nutrient availability and a pathogen-specific immune response.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
N-Acetilglucosaminiltransferases
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Caenorhabditis elegans
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Imunidade Inata
Idioma:
En
Ano de publicação:
2014
Tipo de documento:
Article