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Komagataella pastoris

ABSTRACT: Yeast that widely used in production of recombinant proteins

PROVIDER: PRJNA12846 | ENA |

REPOSITORIES: ENA

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			Action	DRS
		Other
	CABH01.dat.gz	Other
	CABH01.fasta.gz	Fasta.gz
	CABH01.master.dat	Other
	JAPTHC01.dat.gz	Other

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CRISPR-Cas9 knockout screen informs efficient reduction of the Komagataella phaffii secretome

Project description:The yeast Komagataella phaffii is a promising alternative host for manufacturing of therapeutic proteins. Deletion of unneeded endogenous proteins could increase the secreted titer of recombinant proteins by redirecting cellular resources. Genetic engineering in non-model hosts is hampered by limited annotation of genes, especially essential genes. In this study, we identified the set of endogenous secreted proteins in K. phaffii and attempted to disrupt these genes. We designed, transformed, and sequenced a pooled CRISPR-Cas9 knockout library to determine which genes are essential. With this knowledge, we rapidly disrupted up to 9 consecutive genes in K. phaffii. Engineered strains exhibited a ~20x increase in the production of human serum albumin and a 2x increase in the production of a monoclonal antibody. The pooled CRISPR-Cas9 library and knowledge of gene essentiality reported here will facilitate future efforts to engineer K. phaffii for production of other recombinant therapeutic proteins and enzymes.

2024-08-08 | GSE252605 | GEO

Comparison of gene expression profile among Pichia pastoris strain with a different gene dosage

Project description:Pichia pastoris is a widely used yeast platform for heterologous protein production. Although increasing gene dosage is a powerful strategy to improve recombinant protein production, an excess in the number of gene copies often leads to decreased product yields and increased metabolic burden. In order to find the bottlenecks of this strategy, here we present a transcriptome profile comparison of a series of Pichia pastoris strains carrying a different gene dosage of the Rhizopus oryzae lipase (Rol) as a model protein. Cells were grown on a mixture of glycerol:methanol in chemostat cultures. 2 color experiment in reference design.

2017-02-22 | E-MTAB-4582 | biostudies-arrayexpress

Development of a general defined media for Pichia pastoris

Project description:Pichia pastoris is widely used as a host for recombinant protein production. More than 500 proteins have been expressed in the organism at a variety of cultivation scales, from small shake flasks to large bioreactors. Large-scale fermentation strategies typically employ chemically-defined growth media because of its greater batch-to-batch consistency and in many cases, lower cost compared to complex media. For biopharmaceuticals, defined growth media may also simplify downstream purification and regulatory documentation. Standard formulations of defined media for Pichia are minimal ones that lack the metabolic intermediates provided by complex components such as peptone and yeast extract. As a result, growth rates and per-cell productivities are significantly lower than in complex media. We have designed an improved defined media for Pichia pastoris, rich defined medium (RDM), by systematically evaluating nutrients of increasing complexity and identifying those that are most critical for growth. We have also demonstrated the use of RDM for expression of three heterologous proteins, at titers comparable to or higher than in standard complex medium. Rich defined medium has the potential to improve productivity of Pichia pastoris fermentations and accelerate process development for new molecules.

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RNA-seq data from three Saccharomyces cerevisiae strains with different protein productivity

Project description:The budding yeast Saccharomyces cerevisiae is a popular host to be used to produce recombinant proteins. Here we studied three yeast strains with different productivity using the RNA-seq data to elucidate the mechanisms for improving protein production.

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N-glycosylation site occupancy in human prostaglandin H synthases expressed in Pichia pastoris

Project description:Prostaglandin H synthases (PGHSs) are N-glycosylated membrane proteins that catalyse the committed step in prostaglandin synthesis. Unlike PGHS-2, the production of recombinant PGHS-1 in non-mammalian expression systems is complicated. The majority of the heterologous enzyme is inactive due to misfolding. N-glycosylation is proposed to be obligatory for the correct folding of mammalian PGHSs. In this study, human PGHS-1 and -2 (hPGHS-1 and -2) were expressed in the yeast Pichia pastoris, and the N-glycosylation patterns of the purified recombinant proteins were characterised using nano-LC/MS/MS. Recombinant hPGHS-2 was catalytically active, whereas hPGHS-1 was inactive. Unexpectedly, the accumulation of non-glycosylated hPGHS-1 was not observed in the crude lysate of the yeast cells. In addition, the purified hPGHS isoforms exhibited similar N-glycosylation site occupancy. The results indicate that there are more complex grounds for the inactivity of the recombinant hPGHS-1 produced in yeast.

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