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

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

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 …

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

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

Of the many post-translational modifications proteins can undergo, glycosylation is the most
prevalent and the most diverse. Today, it is clear that both N-glycosylation and O …

Protein glycosylation is widespread throughout all three domains of life. Bacterial protein N-
glycosylation and its application to engineering recombinant glycoproteins continue to be …

Glycosylation of proteins is one of the most prevalent post-translational modifications
occurring in nature, with a wide repertoire of biological implications. Pathways for the main …

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