Glycoproteomics: a powerful tool for characterizing the diverse glycoforms of bacterial pilins and flagellins.

With glycosylation now firmly established across both Archaeal and bacterial proteins, a wide array of glycan diversity has become evident from structural analysis and genomic data. These discoveries have been built in part on the development and application of mass spectrometric technologies to the bacterial glycoproteome. This review highlights recent findings using high sensitivity MS of the large variation of glycans that have been reported on flagellin and pilin proteins of bacteria, using both 'top down' and 'bottom up' approaches to the characterization of these glycoproteins. We summarize current knowledge of the sugar modifications that have been observed on flagellins and pilins, in terms of both the diverse repertoire of monosaccharides observed, and the assemblage of moieties that decorate many of these sugars.

N-linked glycosylation in bacteria: an unexpected application.

Traditionally, glycoproteins have been considered the exclusive property of eukaryotes and archaea, but it is now evident that glycoproteins are found in all domains of life. In recent years N-linked glycosylation among some epsilon-proteobacteria has emerged as a new and exciting research area and represents a useful model to understand this complex process in simple, genetically tractable bacteria. Above all, the transfer of N-linked glycosylation systems to the work-horse bacterium, Escherichia coli, has enabled, for the first time, the production of recombinant glycoproteins. This has potentially provided the option for tailor-made glycoproteins and has opened up the field of glycoengineering, particularly with respect to the development of glycoconjugate vaccines.