Conserved nutrient sensor O-GlcNAc transferase is integral to C. elegans pathogen-specific immunity.
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....
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Public Library of Science (PLoS)
2014-01-01
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Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC4256294?pdf=render |
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author | Michelle R Bond Salil K Ghosh Peng Wang John A Hanover |
author_facet | Michelle R Bond Salil K Ghosh Peng Wang John A Hanover |
author_sort | Michelle R Bond |
collection | DOAJ |
description | 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. |
first_indexed | 2024-12-19T19:50:08Z |
format | Article |
id | doaj.art-946fee2d1f324070aeb4a2fddf323a30 |
institution | Directory Open Access Journal |
issn | 1932-6203 |
language | English |
last_indexed | 2024-12-19T19:50:08Z |
publishDate | 2014-01-01 |
publisher | Public Library of Science (PLoS) |
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series | PLoS ONE |
spelling | doaj.art-946fee2d1f324070aeb4a2fddf323a302022-12-21T20:08:02ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-01912e11323110.1371/journal.pone.0113231Conserved nutrient sensor O-GlcNAc transferase is integral to C. elegans pathogen-specific immunity.Michelle R BondSalil K GhoshPeng WangJohn A HanoverDiscriminating 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.http://europepmc.org/articles/PMC4256294?pdf=render |
spellingShingle | Michelle R Bond Salil K Ghosh Peng Wang John A Hanover Conserved nutrient sensor O-GlcNAc transferase is integral to C. elegans pathogen-specific immunity. PLoS ONE |
title | Conserved nutrient sensor O-GlcNAc transferase is integral to C. elegans pathogen-specific immunity. |
title_full | Conserved nutrient sensor O-GlcNAc transferase is integral to C. elegans pathogen-specific immunity. |
title_fullStr | Conserved nutrient sensor O-GlcNAc transferase is integral to C. elegans pathogen-specific immunity. |
title_full_unstemmed | Conserved nutrient sensor O-GlcNAc transferase is integral to C. elegans pathogen-specific immunity. |
title_short | Conserved nutrient sensor O-GlcNAc transferase is integral to C. elegans pathogen-specific immunity. |
title_sort | conserved nutrient sensor o glcnac transferase is integral to c elegans pathogen specific immunity |
url | http://europepmc.org/articles/PMC4256294?pdf=render |
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