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
