Recombinant protein expression in Pichia pastoris

  title={Recombinant protein expression in Pichia pastoris},
  author={James Michael Cregg and Joan Lin Cereghino and Jianying Shi and David R. Higgins},
  journal={Molecular Biotechnology},
The methylotrophic yeast Pichia pastoris is now one of the standard tools used in molecular biology for the generation of recombinant protein. P. pastoris has demonstrated its most powerful success as a large-scale (fermentation) recombinant protein production tool. What began more than 20 years ago as a program to convert abundant methanol to a protein source for animal feed has been developed into what is today two important biological tools: a model eukaryote used in cell biology research… 

Strains and molecular tools for recombinant protein production in Pichia pastoris.

This chapter reviews common and new "Pichia tools" and their specific features, special focus is given to expression strains, such as different methanol utilization, protease-deficient or glycoengineered strains, combined with application highlights.

Genome sequence of the recombinant protein production host Pichia pastoris

The methylotrophic yeast P. pastoris strains capable of human-type N-glycosylation are now available, which increases the utility of this organism for biopharmaceutical production.

Strategies for Optimization Expression of Heterologous Protein in Pichia pastoris

Strategies for reducing proteolytic degradation and improving production of the expressed heterologous proteins are briefly summarized in terms of genetically factors and cultivation level.

Production of recombinant protein in Pichia pastoris by fermentation

This protocol is applicable to recombinant protein expression by small-scale fermentation using the Pichia pastoris expression system. P. pastoris has the capacity to produce large quantities of

Methods for efficient high-throughput screening of protein expression in recombinant Pichia pastoris strains.

Methods to detect and analyze protein expression, developed in a 96-well format for high-throughput screening of recombinant P. pastoris strains are described.

Expression of recombinant proteins in the methylotrophic yeast Pichia pastoris.

The vector used here (pPICZalphaA) contains the AOX1 promoter for tightly regulated, methanol-induced expression of the gene of interest, the alpha-factor secretion signal for secretion of the recombinant protein, a Zeocin resistance gene for selection in both E. coli and Pichia and a polyhistidine tag for detection and purification of a recombinantprotein.

Pichia pastoris: A notable heterologous expression system for the production of foreign proteins—Vaccines

Yeast expression systems are expanding the role of yeast in the process of understanding and engineering eukaryotic proteins, and Pichia pastoris has become a highly popular expression host for the production of a wide variety of intracellular and extracellular recombinant proteins of interest.

Production of Humanlike Recombinant Proteins in Pichia pastoris

Renewed interest in yeast and fungal expression systems in general and the P. pastoris expression system in particular has been spurred by a growing demand for scalable and costeffective humanlike therapeutic protein manufacturing systems.

Heterologous protein production using the Pichia pastoris expression system

The Pichia pastoris expression system is being used successfully for the production of various recombinant heterologous proteins and the importance of optimizing the physicochemical environment for efficient and maximal recombinant protein production in bioreactors and the role of process control in optimizing protein production is reviewed.



Heterologous protein expression in the methylotrophic yeast Pichia pastoris.

This paper reviews the P. pastoris expression system: how it was developed, how it works, and what proteins have been produced and describes new promoters and auxotrophic marker/host strain combinations which extend the usefulness of the system.

Recent Advances in the Expression of Foreign Genes in Pichia pastoris

The Pichia pastoris heterologous gene expression system has been utilized to produce attractive levels of a variety of intracellular and extracellular proteins of interest and improvements in understanding and application have improved its utility even further.

Production of foreign proteins in the yeast Pichia pastoris

The methanol-utilizing yeast Pichia pastoris has been developed as a host system for the production of heterologous proteins of commercial interest and is particularly attractive for the secretion of foreign-gene expression cassette.

Overview of Protein Expression in Pichia pastoris

  • D. Higgins
  • Biology
    Current protocols in protein science
  • 2001
Important considerations for the use of Pichia pastoris are discussed, including strains for expression, expression plasmids, transformation by integration, and post‐translational modifications.

Development of the methylotrophic yeast Pichia methanolica for the expression of the 65 kilodalton isoform of human glutamate decarboxylase

We describe a protein expression system in the methylotrophic yeast, Pichia methanolica. Methods for transformation and genetic manipulation of the organism were developed using an ade2 strain and