Concepts and principles of glycobiology

  title={Concepts and principles of glycobiology},
  author={Ghislain Opdenakker and Pauline M. Rudd and Chris Paul Ponting and Raymond A. Dwek},
  journal={The FASEB Journal},
  pages={1330 - 1337}
In biological systems oligosaccharides are normally conjugated to proteins or lipids. The heterogeneity and branching of oligosaccharides allow glycoconjugates to display a further level of structural and functional diversity compared with linear proteins and nucleic acids or with lipids. This review summarizes some general principles that are emerging from the new field of glycobiology which, by addressing the molecular interactions of glycoconjugates in biological systems, spans the classical… 

Thiyl glycosylation of olefinic proteins: S-linked glycoconjugate synthesis.

The development of a convergent approach for the synthesis of a novel class of S-linked glyconjugate proteins through the site-specific ligation of 1glycosyl thiols to proteins is described, allowing the potential for orthogonal use in combined, multireaction protein chemistry strategies.

Concepts and principles of O-linked glycosylation.

The biosynthesis, structures, and functions of O-glycosylation, as a complex posttranslational event, is reviewed and compared and the recent development of novel technologies for glycan analysis promises to yield new insights in the factors that determine site occupancy, structure-function relationship, and the contribution of O -linked sugars to physiological and pathological processes.

Glycoproteomics: protein modifications for versatile functions. Meeting on glycoproteomics.

Various aspects of the structure–function relationship of glycoproteins were discussed, with an emphasis on the roles of glycans in the development of numerous pathological conditions, as well as in pathogen–host interactions.

Glycobiology in Medicine.

  • Y. LeeR. Lee
  • Biology, Chemistry
    Journal of biomedical science
  • 1996
Conjugation of polysaccharides derived from pathogenic micro-organisms with appropriate proteins provides effective vaccines against the micro- organisms and many pathogens use carbohydrates as recognition markers for invasion.


The increased understanding of the important roles oligosaccharides and glycoconjugates play in fundamental life-sustaining processes has stimulated a need for access to usable quantities of these materials, and developments in synthetic carbohydrate chemistry have centered on finding solutions to two important challenges.

Binding sugars: from natural lectins to synthetic receptors and engineered neolectins.

From the accumulated knowledge on protein-carbohydrate interactions, it is now possible to use nucleotide and peptide (bio)synthesis for producing new carbohydrate-binding molecules and this approach can also be addressed by boron chemistry and supra-molecular chemistry for the design of fully artificial glycosensors.

Protein glycosylation: implications for in vivo functions and therapeutic applications.

This review summarizes recent development and understanding related to synthesis of glycans, their functions, diseases, and various expression systems and characterization of glycosylation in eukaryotic cells.

Glycoproteomics: protein modifications for versatile functions

This satellite meeting of the Thirtieth FEBS Congress and the Ninth IUBMB Conference was held in Dubrovnik, Croatia, between 28 and 30 June 2005. The conference was organized by G. Lauc, J. Dumic and

Photoaffinity glycoprobes-a new tool for the identification of lectins.

The simplicity of the glycoprobe method enables its application in routine monitoring of changes in lectin activity during various developmental or pathological processes.

Human plasma protein N-glycosylation

This review aims to convey the current state of knowledge on the N-glycosylation of the major plasma glycoproteins alpha-1-acid glycoprotein, alpha-2-HS-glycop protein, and speculate how the individual proteins may contribute to a total plasma N-behavioural profile determined at the released glycan level.



Structures and functions of the sugar chains of glycoproteins.

  • A. Kobata
  • Biology
    European journal of biochemistry
  • 1992
Functional aspects of the sugar chains of glycohormones and of those in the immune system will be described to help others understand this new scientific field called 'glycobiology'.

Possible role for peptide-oligosaccharide interactions in differential oligosaccharide processing at asparagine-107 of the light chain and asparagine-297 of the heavy chain in a monoclonal IgG1 kappa.

It is suggested that the completely bisected nature of the light-chain oligosaccharides comes from a high level of activity of GlcNAc-T-III (the enzyme responsible for the attachment of the bisecting Glc NAc) in the cells producing the IgG.

Tissue‐specific N‐glycosylation, site‐specific oligosaccharide patterns and lentil lectin recognition of rat Thy‐1.

It is suggested that by controlling N‐glycosylation a tissue creates an unique set of glycoforms (same polypeptide but with oligosaccharides that differ either in sequence or disposition).

Structure of a C-type mannose-binding protein complexed with an oligosaccharide

The crystal structure at 1.7 Å resolution of the carbohydrate-recognition domain of rat mannose-binding protein complexed with an oligomannose asparaginyl-oligosaccharide reveals that Ca2+ forms coordination bonds with the carbohydrate ligand.

The conformational effects of N-glycosylation on the tailpiece from serum IgM.

1H-NMR spectroscopy has been used to study the conformation and dynamics of the isolated tailpiece from human serum immunoglobulin M, a 22-residue peptide containing a single asparagine glycosylation site, and various roles for the different glycoforms of the tail peptide are discussed.

Recognition of a cell-surface oligosaccharide of pathogenic Salmonella by an antibody Fab fragment.

The 2.05 angstrom (A) resolution crystal structure of a dodecasaccharide-Fab complex revealed an unusual carbohydrate recognition site, defined by aromatic amino acids and a structured water molecule, rather than the carboxylic acid and amide side chains that are features of transport and other carbohydrate binding proteins.

Oligosaccharides at each glycosylation site make structure-dependent contributions to biological properties of human tissue plasminogen activator.

The effect of altering oligosaccharide structures at sites 184 and 448 of tissue plasminogen activator (tPA) has been examined and dMM treatment was found to increase both the lysine affinity and catalytic activity of tPA.

Influence of Carbohydrate Side Chains on Activity of Tissue-Type Plasminogen Activator

It is suggested that the carbohydrate part of the molecule can influence its biological behavior as distinct alterations in the electrophoretic mobility of the molecules are observed.

Tissue plasminogen activator has an O-linked fucose attached to threonine-61 in the epidermal growth factor domain.

The results indicate that this novel type of glycosylation may be common to the epidermal growth factor domains found in coagulation and fibrinolytic proteins and, therefore, suggest that the modification may have functional significance.

Age-related galactosylation of the N-linked oligosaccharides of human serum IgG

The normal variation in galactosylation with age allows a true assessment of disease-associated changes in this parameter, and raises the possibility that one of the lesions in rheumatoid arthritis is an accelerated aging of the immune system.