Glycoproteins Essay

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1.1.1 Glycoproteins and biosynthesis
1.1.1.1. N-Linked glycoproteins
N-Linked glycoproteins were traditionally considered unique for eukaryotic systems. It was not until more recently that their presences in bacteria and archaea become recognized. N-Glycans in eukaryotes share some common features and have a common core structure. They consist of common monosaccharide units. However, their structures in bacteria and archaea are more diverse and contain both common and rare monosaccharide building blocks.

1.1.1.1.1. N-Linked glycoproteins in eukaryotic systems
N-Glycans in eukaryotic cells have a common Man3GlcNAc2 core linked to the Asparagine (Asn) residue in the Asn-X-Ser/Thr sequons of proteins (where X is an amino acid other than proline) and can be classified to high-mannose, complex, and hybrid three types (Figure 1.1). They are presented on many secreted and membrane-bound glycoproteins.

Figure 1.1 Representative high-mannose, complex, and hybrid type N-glycans.

In Saccharomyces cerevisiae and vertebrates, they are initially synthesized on the cytoplasmic side of the endoplasmic reticulum (ER) membrane, starting with the transfer of N-acetylglucosamine phosphate (GlcNAc-P) from nucleotide-activated sugar donor UDP-GlcNAc to the ER membrane-anchored molecule dolichol phosphate (Dol-P). The dolichol pyrophosphate N-acetylglucosamine (Dol-P-P-GlcNAc) formed is further processed by glycosyltransferases. One GlcNAc and five mannose residues are subsequently added from UDP-GlcNAc and GDP-Man, respectively, generating Man5GlcNAc2-P-P-Dol. This sugar chain is flipped into the luminal side of ER membrane and extended by transfer of four mannose residues from Dol-P-Man and three glucose residues from Dol-P-Glc. The 14-sugar pr...

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...1–4Gal1–3diNAcBac–structure of Neisseria gonorrhoeae pilin is assembled by PglB, PglA and PglE onto Und-P, flipped by PglF to periplasm and transferred by PglO on to the Ser residue of pilin [21]. In an alternative pathway, PglH adds a Glc rather than two Gal residues to diNAcBac. In OST-independent O-glycosylation, glycosyltransferases add monosaccharides to proteins in the cytoplasm and the resulted glycosylated proteins are transported to the outer membrane or secreted by the flagellum [22].

1.1.1.2.3 O-Linked glycoproteins in archaea
The surface (S)-layer glycoproteins of archaea were found to be O-glycosylated. In Halobacterium salinarum, the cell envelope protein is modified with glucosylgalactose disaccharides and (uronic acid, glucose)-galatcotse trisaccharides at several sites [23]. Little is known about the O-glycosylation pathway in archaea at present.

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