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Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
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Conjugated Proteins02:50

Conjugated Proteins

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Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties.
Nucleoproteins are protein complexes that contain nucleic acids, categorized as deoxyribonucleoproteins (DNPs) or ribonucleoproteins (RNPs) respectively. The nucleosome is a typical example of a DNP where nuclear DNA is associated with histone proteins. The major antigen for the Covid-19 virus SARS-CoV is an RNP that is critical...
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Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
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Leaky Scanning02:28

Leaky Scanning

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During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
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Proteoglycans01:05

Proteoglycans

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Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
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Decoding Protein Glycosylation for Better Vaccine and Antibody Development.

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Researchers developed advanced chemoenzymatic methods for synthesizing complex glycans and glycoproteins. These tools accelerate discoveries in glycobiology, leading to improved glycoprotein medicines and vaccines for various diseases.

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Area of Science:

  • Glycobiology
  • Biochemistry
  • Medicinal Chemistry

Background:

  • Glycosylation is a critical post-translational modification influencing protein structure, function, and cellular processes.
  • Aberrant glycosylation is linked to diseases, necessitating a deeper understanding of glycan-receptor interactions.
  • Developing novel tools is essential for precise study and therapeutic targeting of glycosylation.

Purpose of the Study:

  • To highlight advanced glycosylation methodologies developed for novel discoveries in glycobiology.
  • To showcase the translation of these discoveries into innovative therapeutic developments.
  • To provide insights into the impact of glycosylation on biological processes and disease.

Main Methods:

  • Chemoenzymatic synthesis of complex glycans and glycoproteins.
  • Development of programmable one-pot synthesis methods.
  • Creation of glycan microarrays for studying interactions.
  • Cell-based production of engineered glycoproteins.

Main Results:

  • Expedient synthesis of oligosaccharides and glycoproteins achieved.
  • Development of glycan microarrays for interaction studies.
  • Design of low-sugar universal vaccines with broad protective immunity.
  • Optimization of cell-based monoclonal antibody production with humanized Fc-glycosylation for enhanced efficacy.
  • Identification of small-molecule blockades for Siglec-mediated immune checkpoints.

Conclusions:

  • Advanced glycosylation methods drive significant discoveries in glycobiology.
  • These methods accelerate the development of novel glycoprotein therapeutics and vaccines.
  • Future integration with AI prediction promises a paradigm shift in drug discovery and human health.