Prokaryotic glycosylation

Abstract

With the advances of molecular biology and with improved analytical techniques a significant change of perception has taken place regarding prokaryotic glycoproteins. Glycosylation of proteins from prokaryotes is no longer considered a specific feature of certain organisms but has been demonstrated for many archaea and bacteria. Besides the occurrence of glycosylated enzymes, antigens and other cell envelope components, surface layer (S-layer) glycoproteins represent the best-studied examples of glycosylated prokaryotic proteins. They are widely distributed among archaeal wild-type strains, but among bacteria they have been mainly observed with Gram-positive organisms. There is, in general, an enormous increase of reports on the presence of glycosylated proteins among prokaryotes. For their isolation and characterization a great number of methods are available, aiming at the identification of the covalent linkage between the carbohydrate and the polypeptide portion. So far, several differences in structure and biosynthesis have been observed in comparison to eukaryotic glycoproteins. In this review we introduce a protocol which has been successfully applied to the investigation of the complex structures, linkage units, and polypeptide consensus sequences of glycosylated bacterial S-layer proteins.

Viruses as Building Blocks for Materials and Devices

“…Owing to the reducing environment in the bacterial cytoplasm, it is often not feasible for proteins to form disulfide bonds. Eukaryotic post‐translational glycosylation, which is rather important for many functions of the displayed polypeptides,49 is not possible either 50…”

The extracellular biology of the lactobacilli

“…Although protein glycosylation was long believed to be restricted to Eukarya, it is now clear that bacteria can also form protein-attached N-glycans via asparagine residues, as well as O-glycans via threonine and/or serine residues (Messner, 2004;Szymanski & Wren, 2005;Weerapana & Imperiali, 2006;Abu-Qarn et al, 2008). Most studies on bacterial protein glycosylation revealed specific O-glycan attachment to one or two abundant polymeric surface proteins such as flagellins, pilins and S-layer proteins (Schaffer et al, 2001;Benz & Schmidt, 2002;Fletcher et al, 2007). Moreover, a limited number of general glycosylation systems have been described in bacteria, including the Nglycosylation machinery in Campylobacter jejuni and related species (Fig.…”

Identification of Modified Proteins by Mass Spectrometry

“…Until recently most of the protein glycosylation has been found on eucaryotic proteins although now it is more evident that glycosylation in procaryotes combines a much greater diversity of glycan composition, linkage units, and glycosylation sequences on polypeptides (6).…”