Mass spectrometry in the elucidation of the glycoproteome of bacterial pathogens

Robert L.J. Graham, Sonja Hess*

*Corresponding author for this work

Research output: Contribution to journalArticle

11 Citations (Scopus)


Presently some three hundred post-translational modifications are known to occur in bacteria in vivo. Many of these modifications play critical roles in the regulation of proteins and control key biological processes. One of the most predominant modifications, N-and O-glycosylations are now known to be present in bacteria (and archaea) although they were long believed to be limited to eukaryotes. In a number of human pathogens these glycans have been found attached to the surfaces of pilin, flagellin and other surface and secreted proteins where it has been demonstrated that they play a role in the virulence of these bacteria. Mass spectrometry characterization of these glycosylation events has been the enabling key technology for these findings. This review will look at the use of mass spectrometry as a key technology for the detection and mapping of these modifications within microorganisms, with particular reference to the human pathogens, Campylobacter jejuni and Mycobacterium tuberculosis. The overall aim of this review will be to give a basic understanding of the current 'state-of-the-art' of the key techniques, principles and technologies, including bioinformatics tools, involved in the analysis of the glycosylation modifications.

Original languageEnglish
Pages (from-to)57-81
Number of pages25
JournalCurrent Proteomics
Issue number1
Publication statusPublished - 24 Jun 2010
Externally publishedYes


  • Eukaryota
  • Glycosylation
  • Mass spectrometry
  • Mycobacterium tuberculosis
  • Post-translational modifications
  • Prokaryota campylobacter jejuni
  • Proteomics

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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