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Yeast Expression

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Recombinant protein production is a multibillion-dollar market. Among several expression systems, yeast cell factories combine the advantages of being single cells, such as fast growth and easy genetic manipulation, as well as eukaryotic features including a secretory pathway leading to correct protein processing and post-translational modifications. In this respect, especially the engineering of yeast glycosylation to produce glycoproteins of human-like glycan structures is of great interest.

Advantages:

  • Faster, easier and less expensive to grow (than mammalian systems)
  • High level of protein expression (10-100 fold) as compared to that of E.coli
  • Protein can be expressed as secretary protein, which helps in downstream processing and purification of the gene product
  • Post-translational modifications required for human proteins
  • Robust cellular structure
  • Synthesis of complex and multi subunit proteins
  • Fermentation process better for industrial use

Disadvantages:

  • Limited choice of vectors
  • Unresolved biological activity of expressed proteins
  • Presence of active proteases that degrade foreign (expressed) proteins, thereby reducing their yield (a solution to this problem is the construction of yeast strains from which the protease genes have been deleted.)
  • Glycosylation pattern dissimilar to humans

Applications:

  • The surface expression of foreign proteins in yeast is generating substantial interest in applications such as biocatalysis, whole call vaccines, and combinatotial library presentation.
  • Methylotrophic yeast Pichia pastoris in the field of food industry.

Figure 1. Expression of human proteins in yeast can lead to an arrest in cell growth and division, and this can be used as a basis for drug screens. (Julian A. Simon & Antonio Bedalov, 2004)Figure 1. Expression of human proteins in yeast can lead to an arrest in cell growth and division, and this can be used as a basis for drug screens. (Julian A. Simon & Antonio Bedalov, 2004)

Please see Creative Biostructure’s cell-free and cell-based expression services.

Reference:

  1. Schreuder M P et al, 1996. Immobilizing proteins on the surface of yeast cells. Trends Biotechnol, 14, 115-120
  2. Celik E, Calik P (2012) Production of recombinant proteins by yeast cells. Biotechnol Adv 30:1108–1118
  3. Julian A. Simon & Antonio Bedalov, Yeast as a model system for anticancer drug discovery. Nature Reviews Cancer 4, 481-487 (June 2004) | doi:10.1038/nrc1372


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