Abstract
Protein glycosylation had been considered as an eccentricity of a few bacteria. However, through advances in analytical methods and genome sequencing, it is now established that bacteria possess both N-linked and O-linked glycosylation pathways. Both glycosylation pathways can modify multiple proteins, flagellins from Archaea and Eubacteria being one of these. Flagella O-glycosylation has been demonstrated in many polar flagellins from Gram-negative bacteria and in only the Gram-positive genera Clostridium and Listeria. Furthermore, O-glycosylation has also been demonstrated in a limited number of lateral flagellins. In this work, we revised the current advances in flagellar glycosylation from Gram-negative bacteria, focusing on the structural diversity of glycans, the O-linked pathway and the biological function of flagella glycosylation.
Highlights
Protein glycosylation, the covalent attachment of carbohydrates to amino acids, is one of the most common posttranslational modifications in eukaryotic cells
Bacteria of the genus Azospirillum have one polar flagellum when grown in liquid media and additional lateral flagella when grown on solid media
Flagellar glycosylation is no longer a rare event found in only a few bacterial species with little biological relevance
Summary
The covalent attachment of carbohydrates to amino acids, is one of the most common posttranslational modifications in eukaryotic cells. Glycosylated proteins provide mechanisms for the control of signal transduction, protein folding, stability, cell-cell interaction and host immune response. It was considered an exclusively eukaryotic mechanism until the identification of glycoproteins in Halobacterium and Clostridium [1,2]. Glycans can contain distinctly bacterial sugars, such as the amino- and deoxy-monosaccharides pseudaminic acid [5], bacillosamine [6], 2,4-diacetamido-2,4,6-trideoxyhexose (DATDH) [7], and N-acetyl fucosamine [8]. Glycans can be linked at several amino acid residues, usually through linkage to the amide group of asparagine residues in. Some bacteria with inappropriate flagellar glycans cannot colonize their host [5], while in others, glycans on proteins mediate interaction with the host cells or evasion of the host’s immune system [9,10]
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