RRC ID 45692
Author Bond MR, Ghosh SK, Wang P, Hanover JA.
Title Conserved nutrient sensor O-GlcNAc transferase is integral to C. elegans pathogen-specific immunity.
Journal PLoS ONE
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 β-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.
Volume 9(12)
Pages e113231
Published 2014
DOI 10.1371/journal.pone.0113231
PII PONE-D-14-39845
PMID 25474640
PMC PMC4256294
MeSH Acetylglucosamine Animals Caenorhabditis elegans / genetics* Caenorhabditis elegans / immunology* Caenorhabditis elegans / microbiology Food Humans Immunity, Innate / genetics* N-Acetylglucosaminyltransferases / genetics* N-Acetylglucosaminyltransferases / metabolism Signal Transduction / genetics Staphylococcus aureus / immunology Staphylococcus aureus / pathogenicity beta Catenin / genetics beta Catenin / metabolism p38 Mitogen-Activated Protein Kinases / genetics p38 Mitogen-Activated Protein Kinases / metabolism
IF 2.776
Times Cited 4
C.elegans tm3642