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Protein Glycosylation01:25

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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.
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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.
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Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
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Enzymatic Glyco-Modification of Synthetic Membrane Systems.

Dylan Jabeguero1, Lina Siukstaite2, Chunyue Wang3

  • 1Centre de Recherches sur les Macromolécules Végétales (CERMAV), CNRS, University Grenoble Alpes, 38041 Grenoble, France.

Biomolecules
|February 25, 2023
PubMed
Summary

Researchers explored using a soluble glycosyltransferase (LgtC) to create the Gb3 antigen cancer biomarker on synthetic cell membrane models. LgtC successfully modified lactosyl-ceramide into Gb3 on giant unilamellar vesicles and supported lipid bilayers.

Keywords:
LgtCgiant unilamellar vesiclesglobotriaosylceramidemolecular dynamicssupported lipid bilayer

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Area of Science:

  • Biochemistry
  • Membrane Biophysics
  • Synthetic Biology

Background:

  • Glycolipids are crucial membrane components.
  • Gb3 antigen is a significant cancer biomarker.
  • Synthetic membrane models like GUVs and SLBs are valuable for studying membrane-associated processes.

Purpose of the Study:

  • To assess the efficacy of a soluble glycosyltransferase (LgtC) in synthesizing the Gb3 antigen on GUVs and SLBs.
  • To demonstrate the potential of LgtC for creating cancer biomarkers on artificial cell membranes.

Main Methods:

  • Utilized giant unilamellar vesicles (GUVs) and supported lipid bilayers (SLBs) as synthetic membrane models.
  • Employed a soluble glycosyltransferase (LgtC) to transfer galactose residues.
  • Monitored Gb3 synthesis using the B-subunit of Shiga toxin and quartz crystal microbalance with dissipation analysis.
  • Performed molecular dynamics simulations to rationalize experimental findings.

Main Results:

  • Demonstrated that LgtC can utilize lactosyl-ceramide (LacCer) as an acceptor to synthesize Gb3 on both GUVs and SLBs.
  • Showed that transient binding of LgtC to the membrane surface is sufficient for efficient Gb3 synthesis.
  • Confirmed Gb3 formation using Shiga toxin B-subunit binding and QCM-D measurements.

Conclusions:

  • Soluble LgtC can effectively synthesize the Gb3 antigen on synthetic membrane models.
  • This approach holds promise for developing targeted cancer therapies and diagnostics.
  • The study provides insights into enzyme-membrane interactions and glycolipid synthesis.