Mapping phosphoproteins in Neisseria meningitidis serogroup A

Proteomics. 2011 Apr;11(7):1351-8. doi: 10.1002/pmic.201000406. Epub 2011 Feb 17.

Abstract

To investigate the phosphorylation capability of serogroup A Neisseria meningitidis (MenA) and to implement our knowledge in meningococcal biology and in bacterial post-translational modifications, cell extracts were separated by 2-DE and 51 novel phosphoproteins were revealed by the use of the highly specific Ser/Thr/Tyr-phosphorylated proteins staining by Pro-Q Diamond and identified by MALDI-ToF/MS. Our results indicate that phosphorylation in MenA is comparable to that of other bacterial species. A first functional characterization of the identified modified proteins was also given, in order to understand their role in meningococcal physiopathology.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / analysis*
  • Bacterial Proteins / chemistry
  • Cell Extracts / chemistry
  • Electrophoresis, Gel, Two-Dimensional
  • Humans
  • Meningitis, Meningococcal / microbiology
  • Neisseria meningitidis, Serogroup A* / genetics
  • Neisseria meningitidis, Serogroup A* / metabolism
  • Peptide Mapping / methods
  • Phosphoproteins / analysis*
  • Phosphoproteins / chemistry
  • Phosphorylation
  • Protein Processing, Post-Translational
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Staining and Labeling / methods
  • Trypsin / metabolism

Substances

  • Bacterial Proteins
  • Cell Extracts
  • Phosphoproteins
  • Trypsin