Publications by authors named "Manoj K Dooda"
Background: Bacterial surface glycans are assembled by glycosyltransferases (GTs) that transfer sugar monomers to long-chained lipid carriers. Most bacteria employ the 55-carbon chain undecaprenyl phosphate (Und-P) to scaffold glycan assembly. The amount of Und-P available for glycan synthesis is thought to be limited by the rate of Und-P synthesis and by competition for Und-P between phosphoglycosyl transferases (PGTs) and GTs that prime glycan assembly (which we collectively refer to as PGT/GTs).
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- Bacteria utilize various carbohydrates to create a wide array of glycans, with amino sugars like -acetylglucosamine (GlcNAc) being fundamental components of their cell walls and exopolysaccharides.
- By expressing NahK, researchers can bypass the hexosamine pathway and directly introduce an analogue called -azidoacetylglucosamine (GlcNAz) for metabolic labeling, confirmed through fluorescence-assisted gel electrophoresis.
- The study found that GlcNAz was primarily incorporated into peptidoglycan (PGN), with lesser incorporation into other polysaccharides, which provides insights for developing carbohydrate-based probes and metabolic engineering techniques.
Article Synopsis
- Bacteria utilize various carbohydrates to create complex structures called glycans, particularly incorporating amino sugars like -acetylglucosamine (GlcNAc) in their cell walls and exopolysaccharides.
- A method was developed to bypass the bacterial hexosamine pathway by expressing NahK, allowing the introduction of a GlcNAc analogue, -azidoacetylglucosamine (GlcNAz), which was confirmed to produce another compound, UDP-GlcNAz, using gel electrophoresis.
- The study found that GlcNAz was primarily incorporated into peptidoglycan (PGN), while lower levels were seen in poly-β-1,6--acetylglucos