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. 2010:2010:148178.
doi: 10.1155/2010/148178. Epub 2011 Jan 27.

Similarities and differences in the glycosylation mechanisms in prokaryotes and eukaryotes

Anne Dell  1 , Alaa Galadari, Federico Sastre, Paul Hitchen
Affiliations

Similarities and differences in the glycosylation mechanisms in prokaryotes and eukaryotes

Anne Dell et al. Int J Microbiol. 2010.

Abstract

Recent years have witnessed a rapid growth in the number and diversity of prokaryotic proteins shown to carry N- and/or O-glycans, with protein glycosylation now considered as fundamental to the biology of these organisms as it is in eukaryotic systems. This article overviews the major glycosylation pathways that are known to exist in eukarya, bacteria and archaea. These are (i) oligosaccharyltransferase (OST)-mediated N-glycosylation which is abundant in eukarya and archaea, but is restricted to a limited range of bacteria; (ii) stepwise cytoplasmic N-glycosylation that has so far only been confirmed in the bacterial domain; (iii) OST-mediated O-glycosylation which appears to be characteristic of bacteria; and (iv) stepwise O-glycosylation which is common in eukarya and bacteria. A key aim of the review is to integrate information from the three domains of life in order to highlight commonalities in glycosylation processes. We show how the OST-mediated N- and O-glycosylation pathways share cytoplasmic assembly of lipid-linked oligosaccharides, flipping across the ER/periplasmic/cytoplasmic membranes, and transferring "en bloc" to the protein acceptor. Moreover these hallmarks are mirrored in lipopolysaccharide biosynthesis. Like in eukaryotes, stepwise O-glycosylation occurs on diverse bacterial proteins including flagellins, adhesins, autotransporters and lipoproteins, with O-glycosylation chain extension often coupled with secretory mechanisms.

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Figures

Figure 1
Figure 1
This figure highlights similarities between the biosynthetic pathways of N-linked glycosylation in archaea (a) compared to eukarya (b) and bacteria (c). The elongation steps flagged in yellow in (b) do not have counterparts in (a) and (c).
Figure 2
Figure 2
This figure depicts key steps in the LOS and LPS biosynthetic pathway in Gram-negative bacteria which have their parallels in N- and O-glycosylation (Figures 1 and 5). For simplicity, other key steps such as the polymerization of the O-antigen prior to transfer to lipid A involved in LPS biosynthesis are not shown.
Figure 3
Figure 3
Structures of Dolichol phosphate and Undecaprenol phosphate.
Figure 4
Figure 4
Structures of representative examples of bacterial and archaeal N-glycans.
Figure 5
Figure 5
This figure shows key steps in the O-oligosaccharyltransferase-mediated O-glycosylation pathways in Neisseria and Pseudomonas. Note the similarities to N-glycosylation (Figure 1) and LPS biosynthesis (Figure 2).
Figure 6
Figure 6
Comparison of mucin-like sequences in bacteria with mammalian mucins. Partial sequences of Fap1 in S. parasanguinis and MUC 1 in Homo sapiens are shown.
Figure 7
Figure 7
Sequence of the passenger domain of the autotransporter protein Ag43 from E. coli with heptosylation sites indicated in red.
See this image and copyright information in PMC

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