Glycosyl phosphate repeating structures are found in capsular polysaccharides of some of Neisseria meningitidis and Streptococcus pneumoniae and lipophosphoglycans of Leishmania. Although capsular polysaccharides and lipophosphoglycans play immunologically pivotal roles, their synthesis remains challenging. In this research, a glycosyl boranophosphate, where one of the nonbridging oxygen atoms is replaced with a borano group, is focused on as a key compound for the efficient synthesis of glycosyl phosphate derivatives. Moreover, the author developed the stereocontrolled synthesis of glycosyl boranophosphates to leverage them as probes for the functional elucidation of glycosyl phosphates and pharmaceutical candidates.

Endo-β-N-acetylglucosaminidases (ENGases) are endoglycosidases that hydrolyze asparagine-linked glycan on glycoproteins. These enzymes play a crucial role in the structural analysis of glycoprotein glycans due to their hydrolytic activity and facilitate the synthesis of glycoproteins with homogeneous glycan structures through glycosylation activity. In this study, we present an approach to detect the hydrolysis and transglycosylation activities of ENGase using glycan-based molecular probes.

Glycans are sugars/sugar chains that are commonly attached to proteins or lipids where they can influence the physiological and biological properties of the carrier molecules. However, free, unconjugated glycans have also been identified in the cytosol of mammalian cells. Structural characterization of cytosolic free glycans demonstrates that they have structural similarities with N-linked glycans on proteins/lipids and their biosynthetic pathway has been gradually clarified. Recently, free glycans have also been identified in sera of various animal species. These extracellular free glycans also include free N-glycans, which have distinct structural features compared to intracellular free N-glycans, implying that they are formed through a different pathway than intracellular free glycans. In addition to free N-linked glycans, sialyl lactose/N-acetyllactosamine-type free glycans have been identified in the serum. Here, this mini-review briefly summarizes recent progress on understanding the mechanisms by which free glycans in mammalian cells as well as in animal sera are formed.

Glycosyl phosphate repeating structures are found in capsular polysaccharides of some of Neisseria meningitidis and Streptococcus pneumoniae and lipophosphoglycans of Leishmania. Although capsular polysaccharides and lipophosphoglycans play immunologically pivotal roles, their synthesis remains challenging. In this research, a glycosyl boranophosphate, where one of the nonbridging oxygen atoms is replaced with a borano group, is focused on as a key compound for the efficient synthesis of glycosyl phosphate derivatives. Moreover, the author developed the stereocontrolled synthesis of glycosyl boranophosphates to leverage them as probes for the functional elucidation of glycosyl phosphates and pharmaceutical candidates.

Endo-β-N-acetylglucosaminidases (ENGases) are endoglycosidases that hydrolyze asparagine-linked glycan on glycoproteins. These enzymes play a crucial role in the structural analysis of glycoprotein glycans due to their hydrolytic activity and facilitate the synthesis of glycoproteins with homogeneous glycan structures through glycosylation activity. In this study, we present an approach to detect the hydrolysis and transglycosylation activities of ENGase using glycan-based molecular probes.

Glycans are sugars/sugar chains that are commonly attached to proteins or lipids where they can influence the physiological and biological properties of the carrier molecules. However, free, unconjugated glycans have also been identified in the cytosol of mammalian cells. Structural characterization of cytosolic free glycans demonstrates that they have structural similarities with N-linked glycans on proteins/lipids and their biosynthetic pathway has been gradually clarified. Recently, free glycans have also been identified in sera of various animal species. These extracellular free glycans also include free N-glycans, which have distinct structural features compared to intracellular free N-glycans, implying that they are formed through a different pathway than intracellular free glycans. In addition to free N-linked glycans, sialyl lactose/N-acetyllactosamine-type free glycans have been identified in the serum. Here, this mini-review briefly summarizes recent progress on understanding the mechanisms by which free glycans in mammalian cells as well as in animal sera are formed.