Protein glycosylation is an important post-translational modification. It is a feature that
enhances the functional diversity of proteins and influences their biological activity. A wide …

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 …

Pseudomonas aeruginosa causes serious nosocomial infections, and an important
virulence factor produced by this organism is lipopolysaccharide (LPS). This review …

Many biologically active small‐molecule natural products produced by microorganisms
derive their activities from sugar substituents. Changing the structures of these sugars can …

Campylobacter jejuni and Campylobacter coli are among the major causes of diarrheal
disease worldwide. The motility imparted by the polar flagella of these pathogens is required …

Asparagine-linked protein glycosylation is a prevalent protein modification reaction in
eukaryotic systems. This process involves the co-translational transfer of a pre-assembled …

This review covers the O antigens of the 46 serotypes of Shigella, but those of most Shigella
flexneri are variants of one basic structure, leaving 34 Shigella distinct O antigens to review …

Asparagine-linked glycosylation involves the sequential assembly of an oligosaccharide
onto a polyisoprenyl donor, followed by the en bloc transfer of the glycan to particular …

Analysis of the complete flagellin glycosylation locus of Campylobacter jejuni strain 81–176
revealed a less complex genomic organization than the corresponding region in the …

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 …