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Expression of Recombinant Proteins in the Methylotrophic Yeast Pichia pastoris
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Tuning recombinant protein expression to match secretion capacity.

Luminita Gabriela Horga1, Samantha Halliwell1, Tania Selas Castiñeiras2

  • 1Manchester Institute of Biotechnology, School of Chemistry, University of Manchester, Manchester, M1 7DN, UK.

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Controlling recombinant protein expression with RiboTite enhances bacterial secretion capacity. This system maintains cell viability, enabling high-quality production of disulfide-bond proteins and antibody fragments.

Keywords:
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Area of Science:

  • Biotechnology
  • Molecular Biology
  • Microbial Engineering

Background:

  • Secreting disulfide-bond proteins into the periplasm of Gram-negative bacteria offers advantages for isolation, quality, and activity.
  • E. coli secretion machinery has limited capacity, leading to overload, cytoplasmic retention, and reduced cell viability.
  • Fine control of recombinant gene expression can match production to host secretion capacity, preventing overload.

Purpose of the Study:

  • To apply the RiboTite gene expression control system for fine-tuning recombinant protein expression levels.
  • To investigate the impact of controlled expression on host cell viability and product quality.

Main Methods:

  • Utilized the RiboTite gene expression control system.
  • Applied fine control over cellular expression levels of recombinant proteins.
  • Cultured Gram-negative bacteria (E. coli) for protein production.

Main Results:

  • Achieved fine control over cellular expression levels using the RiboTite system.
  • Maintained host cell viability despite recombinant protein production.
  • Enabled production of high-quality, active disulfide-bond containing proteins with enhanced volumetric titres.

Conclusions:

  • The RiboTite system effectively manages recombinant protein expression to avoid host cell overload.
  • Expanded the toolkit for producing disulfide-bond proteins, including antibody fragments, in bacterial hosts.
  • Facilitated improved yields and quality of recombinant proteins through controlled expression.