Overlapping and unique signatures in the proteomic and transcriptomic responses of the nematode Caenorhabditis elegans toward pathogenic Bacillus thuringiensis

Dev Comp Immunol. 2015 Jul;51(1):1-9. doi: 10.1016/j.dci.2015.02.010. Epub 2015 Feb 23.


Pathogen infection can activate multiple signaling cascades that ultimately alter the abundance of molecules in cells. This change can be measured both at the transcript and protein level. Studies analyzing the immune response at both levels are, however, rare. Here, we compare transcriptome and proteome data generated after infection of the nematode and model organism Caenorhabditis elegans with the Gram-positive pathogen Bacillus thuringiensis. Our analysis revealed a high overlap between abundance changes of corresponding transcripts and gene products, especially for genes encoding C-type lectin domain-containing proteins, indicating their particular role in worm immunity. We additionally identified a unique signature at the proteome level, suggesting that the C. elegans response to infection is shaped by changes beyond transcription. Such effects appear to be influenced by AMP-activated protein kinases (AMPKs), which may thus represent previously unknown regulators of C. elegans immune defense.

Keywords: Bacillus thuringiensis; C-type lectins; Caenorhabditis elegans; Innate immunity; Proteomics; RNA-Seq.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Monophosphate / metabolism
  • Animals
  • Bacillus thuringiensis / immunology*
  • Caenorhabditis elegans Proteins / genetics
  • Caenorhabditis elegans Proteins / metabolism*
  • Caenorhabditis elegans*
  • Gene Expression Profiling
  • Gram-Positive Bacterial Infections / immunology*
  • Host-Pathogen Interactions / genetics
  • Immunity, Innate / genetics
  • Lectins, C-Type / genetics
  • Protein Kinases / metabolism*
  • Proteome
  • RNA Processing, Post-Transcriptional
  • Species Specificity
  • Transcriptome


  • Caenorhabditis elegans Proteins
  • Lectins, C-Type
  • Proteome
  • Adenosine Monophosphate
  • Protein Kinases