Glycoproteins: Chemical Features and Biological Roles

Li, Yanhong; Li, Xixuan; Chen, Xi

doi:10.1142/9781783267200_0001

Cited by 2 publications

(3 citation statements)

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“…Protein glycosylation was once considered as the event only reserved in eukaryotic systems. However, recent discoveries have shown that protein glycosylation is also a common phenomenon in some microorganisms, including bacteria, archaea, and fungi. , In contrast to most other PTMs, such as phosphorylation, that usually involve a simple functional group transfer to one or a handful of amino acid residues, glycosylation can be much more complex and structurally and functionally diverse. , So far, over 40 different types of the sugar-amino acid junctions have been identified that involve at least 8 different amino acid residues and 13 different proximal monosaccharides. , While microorganisms are found to have diverse rare monosaccharide units in secondary metabolites, surprisingly only a dozen or so common monosaccharides are present in typical eukaryotic glycoproteins (Figure ). Nevertheless, the limited numbers of building blocks can still form incredibly diverse structures due to the huge possibilities of linkage types, anomeric stereochemistry, and/or additional noncarbohydrate decorations of the sugar chains.…”

Section: General Aspects Of the Structure Function And Synthesis Of G...mentioning

confidence: 99%

Chemoenzymatic Methods for the Synthesis of Glycoproteins

2018

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Glycosylation is one of the most prevalent posttranslational modifications that profoundly affects the structure and functions of proteins in a wide variety of biological recognition events. However, the structural complexity and heterogeneity of glycoproteins, usually resulting from the variations of glycan components and/or the sites of glycosylation, often complicates detailed structure-function relationship studies and hampers the therapeutic applications of glycoproteins. To address these challenges, various chemical and biological strategies have been developed for producing glycan-defined homogeneous glycoproteins. This review highlights recent advances in the development of chemoenzymatic methods for synthesizing homogeneous glycoproteins, including the generation of various glycosynthases for synthetic purposes, endoglycosidase-catalyzed glycoprotein synthesis and glycan remodeling, and direct enzymatic glycosylation of polypeptides and proteins. The scope, limitation, and future directions of each method are discussed.

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Section: General Aspects Of the Structure Function And Synthesis Of G...mentioning

confidence: 99%

Chemoenzymatic Methods for the Synthesis of Glycoproteins

2018

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“…Glycoprotein N-glycans are attached via the innermost N -acetylglucosamine residue to the L-asparagine residue (GlcNAcβ1–Asn) in the Asn-X-Ser/Thr sequon (where X is an amino acid that is not an L-proline) of the protein with a β-linked N-glycosidic bond. All eukaryotic glycoprotein N-glycans share a trimannosyl chitobiose (Man 3 GlcNAc 2 ) core and can be classified as high-mannose, complex, and hybrid types based on the glycan structures extended from the terminal mannose residues on the core [ 1 , 2 ].…”

Section: Introductionmentioning

confidence: 99%

“…Many therapeutic proteins and enzymes are N-glycosylated. The level of N-glycosylation and the structure of their N-glycans can directly affect their solubility, stability, safety, function, efficacy, delivery, pharmacokinetics, immunogenicity, and dose frequency [ 1 , 3 , 4 , 5 , 6 , 7 , 8 , 9 ]. Therefore, N-glycosylation is a critical quality attribute (CQA) of glycoprotein therapeutics considered by regulatory authorities [ 3 , 5 , 10 ].…”

Section: Introductionmentioning

confidence: 99%

Glycoprotein In Vitro N-Glycan Processing Using Enzymes Expressed in E. coli

Zhang

et al. 2023

Molecules

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Protein N-glycosylation is a common post-translational modification that plays significant roles on the structure, property, and function of glycoproteins. Due to N-glycan heterogeneity of naturally occurring glycoproteins, the functions of specific N-glycans on a particular glycoprotein are not always clear. Glycoprotein in vitro N-glycan engineering using purified recombinant enzymes is an attractive strategy to produce glycoproteins with homogeneous N-glycoforms to elucidate the specific functions of N-glycans and develop better glycoprotein therapeutics. Toward this goal, we have successfully expressed in E. coli glycoside hydrolases and glycosyltransferases from bacterial and human origins and developed a robust enzymatic platform for in vitro processing glycoprotein N-glycans from high-mannose-type to α2–6- or α2–3-disialylated biantennary complex type. The recombinant enzymes are highly efficient in step-wise or one-pot reactions. The platform can find broad applications in N-glycan engineering of therapeutic glycoproteins.

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Glycoproteins: Chemical Features and Biological Roles

Cited by 2 publications

References 104 publications

Chemoenzymatic Methods for the Synthesis of Glycoproteins

Chemoenzymatic Methods for the Synthesis of Glycoproteins

Glycoprotein In Vitro N-Glycan Processing Using Enzymes Expressed in E. coli

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