High-coverage proteome analysis reveals the first insight of protein modification systems in the pathogenic spirochete Leptospira interrogans

Cell Res. 2010 Feb;20(2):197-210. doi: 10.1038/cr.2009.127. Epub 2009 Nov 17.


Leptospirosis is a widespread zoonotic disease caused by pathogenic spirochetes of the genus Leptospira that infects humans and a wide range of animals. By combining computational prediction and high-accuracy tandem mass spectra, we revised the genome annotation of Leptospira interrogans serovar Lai, a free-living pathogenic spirochete responsible for leptospirosis, providing substantial peptide evidence for novel genes and new gene boundaries. Subsequently, we presented a high-coverage proteome analysis of protein expression and multiple posttranslational modifications (PTMs). Approximately 64.3% of the predicted L. interrogans proteins were cataloged by detecting 2 540 proteins. Meanwhile, a profile of multiple PTMs was concurrently established, containing in total 32 phosphorylated, 46 acetylated and 155 methylated proteins. The PTM systems in the serovar Lai show unique features. Unique eukaryotic-like features of L. interrogans protein modifications were demonstrated in both phosphorylation and arginine methylation. This systematic analysis provides not only comprehensive information of high-coverage protein expression and multiple modifications in prokaryotes but also a view suggesting that the evolutionarily primitive L. interrogans shares significant similarities in protein modification systems with eukaryotes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Acetyltransferases / metabolism
  • Algorithms
  • Amino Acid Sequence
  • Animals
  • Bacterial Proteins / metabolism
  • Base Sequence
  • Genome, Bacterial
  • Leptospira interrogans / genetics
  • Leptospira interrogans / metabolism*
  • Molecular Sequence Data
  • Phosphorylation
  • Protein Kinases / metabolism
  • Protein Processing, Post-Translational* / physiology
  • Proteome / analysis*
  • Proteomics / methods
  • Sequence Homology, Amino Acid
  • Spirochaetales / genetics
  • Spirochaetales / metabolism
  • Tandem Mass Spectrometry


  • Bacterial Proteins
  • Proteome
  • Acetyltransferases
  • Protein Kinases