In eukaryotes, the combinatorial potential of carbohydrates is used for the modulation of
protein function. However, despite the wealth of cell wall and surface-associated …

Glycosylation is a ubiquitous process that is universally conserved in nature. The various
products of glycosylation, such as polysaccharides, glycoproteins, and glycolipids, perform a …

Bacterial protein glycosylation is an important post-translational modification that can
distinguish pathogenic bacteria from human cells. This review discusses recent findings in …

Bacterial surfaces are rich in glycoconjugates such as capsules, lipopolysaccharides, and
peptidoglycans. The discovery of prokaryotic protein glycosylation systems has revealed that …

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 …

In eukaryotes, glycosylated proteins are ubiquitous components of extracellular matrices
and cellular surfaces. Their oligosaccharide moieties are implicated in a wide range of cell …

Pathogenic bacteria encode virulent glycosyltransferases that conjugate various glycans
onto substrate proteins via the N-or O-linkage. The HMW system in nontypeable …

Glycosylated proteins are ubiquitous components of eukaryote cellular surfaces, where the
glycan moieties are implicated in a wide range of cell–cell recognition events. Once thought …

In recent years, accumulating evidence for glycosylated bacterial proteins has overthrown
an almost dogmatic belief that prokaryotes are not able to synthesize glycoproteins. Now it is …

Although widely distributed in eukaryotic cells glycoproteins appear to be rare in prokaryotic
organisms. The prevalence of the misconception that bacteria do not glycosylate their …