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  • Review Article
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Protein glycosylation in bacteria: sweeter than ever

Nature Reviews Microbiology volume 8, pages 765–778 (2010)Cite this article

Subjects

Key Points

  • Recent progress has been made in understanding N-linked protein glycosylation in Campylobacter jejuni.

  • New N-glycosylation pathways similar to that found in C. jejuni have now been identified in other species.

  • A new N-glycosylation pathway in Haemophilus influenzae has been characterized and found to function in the bacterial cytoplasm; this pathway does not involve block transfer of sugars from a lipid carrier.

  • Bacterial O-glycosylation pathways have also been studied, with a focus on flagellin and pilin modification systems.

  • Recently, it has been demonstrated that particular bacterial O-glycosylation pathways also modify multiple proteins with glycans transferred en bloc from a lipid carrier.

  • Bacterial protein modification has an important biological role. Furthermore, these biosynthesis pathways can be manipulated to engineer recombinant glycoproteins with potential commercial value, and there are several emerging methods for the characterization of these systems.

Abstract

Investigations into bacterial protein glycosylation continue to progress rapidly. It is now established that bacteria possess both N-linked and O-linked glycosylation pathways that display many commonalities with their eukaryotic and archaeal counterparts as well as some unexpected variations. In bacteria, protein glycosylation is not restricted to pathogens but also exists in commensal organisms such as certain Bacteroides species, and both the N-linked and O-linked glycosylation pathways can modify multiple proteins. Improving our understanding of the intricacies of bacterial protein glycosylation systems should lead to new opportunities to manipulate these pathways in order to engineer glycoproteins with potential value as novel vaccines.

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Figure 1: Overview of bacterial N-linked pathways for protein glycosylation.
Figure 2: Phylogenetic tree comparing protein glycosylation B (PglB) sequences of all sequenced deltaproteobacteria and epsilonproteobacteria.
Figure 3: Organization of selected N-linked protein glycosylation gene clusters.
Figure 4: Overview of bacterial O-linked pathways for protein glycosylation.

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Acknowledgements

We thank W. G. Miller for providing sequence information on the pgl loci, and M. Klotz and J. St.Geme for stimulating discussions. This work has been supported by the Alberta Ingenuity Centre for Carbohydrate Science and the Canadian National Research Council Genomics and Health Initiative. C.M.S. is an Alberta Ingenuity Scholar.

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  1. Department of Biological Sciences and the Alberta Ingenuity Centre for Carbohydrate Science, University of Alberta, Edmonton, T6G 2E9, Alberta, Canada

    Harald Nothaft & Christine M. Szymanski

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S-layer

Two-dimensional array of protein or glycoprotein subunits, each with molecular masses ranging from 40 to 200 kDa, that are common constituents of bacterial cell walls.

Competence

The ability of a bacterium to take up extracellular DNA.

Two-partner secretion system

Form of type V secretion system comprising two distinct proteins: a transporter and a secreted effector.

Slipped-strand mispairing

Mispairing of tandem direct repeat DNA that occurs owing to slippage between the template and newly synthesized DNA strands during replication. Such mispairing can change the number of repeats in the newly synthesised strand relative to the template DNA.

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Nothaft, H., Szymanski, C. Protein glycosylation in bacteria: sweeter than ever. Nat Rev Microbiol 8, 765–778 (2010). https://doi.org/10.1038/nrmicro2383

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