Therapeutic glycoproteins have occupied an extremely important position in the market of biopharmaceuticals. Due to the ability of performing posttranslational modifications (PTM) and secreting the target protein to the cultivation broth, the methylotrophic yeast Pichia pastoris is widely used for glycoprotein production in biotechnology and biopharmaceutical industry. With Ph.D. level scientists and over a decade of experience in recombinant protein production, Creative Biolabs has successfully constructed a glyco-engineered P. pastoris to produce high-quality glycoproteins, which are similar to human.

Introduction of P. pastoris

P. pastoris, which belongs to the genus Komagataella spp, is an organism commonly employed to produce a variety of active proteins with N- /O-linked glycans. This expression system has the characteristics of fast growth, easy cultivation, simple genetic manipulation, and the ability to perform space folding and glycosylation of proteins. The glycans of the P. pastoris-produced proteins is high-mannose type without core fucose, leading to reduced in vivo half-life and biological activity, and besides, carrying high mannose chains, glycoproteins cause an immune response in the body. Due to the shortcomings of excessive glycosylation modification of this expression system, it cannot replace mammalian cells to produce various glycoproteins. Therefore, solving the problem of high mannose chain is the core step of glycosylation engineering of P. pastoris.

Glyco-engineered Pichia pastoris Expression System

Glyco-engineered P. pastoris for Glycoprotein Production at Creative Biolabs

Based on our cutting-edge genetic engineering technology, our scientists have modified the glycosylation pathway of P. pastoris by knocking out the och1 gene and introducing mannosidase and successfully constructed a glycoengineered P. pastoris expression system, with obvious advantages, including short production period, low cost, high yield, easy operation and scaling up. This expression system overcomes the disadvantage of excessive glycosylation of proteins to form high mannose chains in wild-type P. pastoris, allowing the production of glycoproteins with uniform low molecular sugar chains. This new type of expression system combines the advantages of Escherichia coli, mammalian cells, and yeast, and overcomes their shortcomings, making it a good choice for glycoprotein production.

Our Services Including but Not Limited to:

  • Sequence design of the gene sequence of target glycoprotein, codon optimization, and gene synthesis;
  • Expression vector construction;
  • Transformation and identification of positive strains by PCR;
  • Select positive strains for protein expression identification;
  • Large-scale culture and purification.

Highlights

  • Production of glycoproteins with uniform low molecular glycan chains
  • Production of glycoproteins with the natural state biological activity
  • Short production period, high yield, easy operation and scaling up
  • Ensuring the amount and purity of glycoprotein delivered
  • High flexibility and cost-effectiveness

With abundant experience and comprehensive powerful platforms for glycoprotein production, Creative Biolabs is a perfect partner to offer our clients high-quality glycoproteins to facilitate our customers’ research and project development. For more detailed information, please feel free to contact us or directly send us an inquiry.

Reference

  1. Ye, J.; et al. Optimization of a glycoengineered Pichia pastoris cultivation process for commercial antibody production. Biotechnology progress. 2011, 27(6): 1744-50.

Related Services:

  1. Glyco-engineered Mammalian Cell Expression System
  2. Glyco-engineered Plant-based Expression System
  3. Therapeutic Glycoprotein Development
  4. Glycoengineering of Antibody
  5. Cell Line Glycoengineering

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