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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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Protein Engineering by Yeast Surface Display
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Recent Advances Toward Engineering Glycoproteins Using Modified Yeast Display Platforms.

Anjali Shenoy1, Adam W Barb2

  • 1Biochemistry and Molecular Biology Department, University of Georgia, Athens, GA, USA.

Methods in Molecular Biology (Clifton, N.J.)
|October 6, 2021
PubMed
Summary

Advanced yeast strains enable glycoprotein engineering for improved recombinant protein expression. These platforms overcome limitations of traditional yeast surface display (YSD) for better glycoprotein diversification and function.

Keywords:
GlycoengineeringGlycosylhydrolaseGlycosyltransferaseYeast surface display

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Area of Science:

  • Biotechnology
  • Molecular Biology
  • Protein Engineering

Background:

  • Yeast are valuable for recombinant protein expression, offering eukaryotic post-translational modifications like N-glycosylation.
  • Traditional yeast surface display (YSD) faces limitations in glycoprotein diversification due to excessive mannose residues, potentially obscuring epitopes and causing immunogenicity.

Purpose of the Study:

  • To review advancements in yeast expression platforms for glycoprotein engineering.
  • To assess the suitability of these advanced platforms for yeast surface display (YSD) of functional glycoproteins.

Main Methods:

  • Development of yeast strains with 'humanized' N-glycosylation machinery by targeting specific enzymes.
  • Engineering of advanced yeast strains to provide essential glycan modifications at termini.
  • Review of existing literature on yeast expression platforms for glycoprotein engineering.

Main Results:

  • Early knockout strains showed morphological defects and poor growth.
  • Humanized glycosylation strains overcame limitations, enabling better glycoprotein diversification.
  • Advanced yeast strains facilitate crucial glycan modifications for full glycoprotein function.

Conclusions:

  • Advanced yeast expression platforms are crucial for overcoming limitations in traditional YSD for glycoprotein engineering.
  • These platforms offer improved strategies for producing functional glycoproteins with tailored glycosylation patterns.
  • Further development is needed to fully leverage these platforms for diverse glycoprotein applications.