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Multiplex secretome engineering enhances recombinant protein production and purity

ABSTRACT: Multiplex secretome engineering enhances recombinant protein production and purity

PROVIDER: PRJNA604220 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR10995700_1.fastq.gz	Fastqsanger.gz
	SRR10995700_2.fastq.gz	Fastqsanger.gz
	SRR10995701_1.fastq.gz	Fastqsanger.gz
	SRR10995701_2.fastq.gz	Fastqsanger.gz
	SRR10995702_1.fastq.gz	Fastqsanger.gz

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Multiplex secretome engineering enhances recombinant protein production and purity

Project description:Host cell proteins (HCPs) are process-related impurities generated during biotherapeutic protein production. HCPs can be problematic if they pose a significant metabolic demand, degrade product quality, or contaminate the final product. Here, we present an effort to create a “clean” Chinese hamster ovary (CHO) cell by disrupting multiple genes to eliminate HCPs. Using a model of CHO cell protein secretion, we predicted the elimination of unnecessary HCPs could have a non-negligible impact on protein production. We analyzed the total HCP content of 6-protein, 11-protein, and 14-protein knockout clones and characterized their growth in shake flasks and bioreactors. These cell lines exhibited a substantial reduction in total HCP content (40%-70%). We also observed higher productivity and improved growth characteristics, in specific clones. With the reduced HCP content, protein A and ion exchange chromatography more efficiently purified a monoclonal antibody (mAb) produced in these cells during a three-step purification process. Thus, substantial improvements can be made in protein titer and purity through large-scale HCP deletion, providing an avenue to increased quality and affordability of high-value biopharmaceuticals.

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Multiplex secretome engineering enhances recombinant protein production and purity.

Project description:Host cell proteins (HCPs) are process-related impurities generated during biotherapeutic protein production. HCPs can be problematic if they pose a significant metabolic demand, degrade product quality, or contaminate the final product. Here, we present an effort to create a "clean" Chinese hamster ovary (CHO) cell by disrupting multiple genes to eliminate HCPs. Using a model of CHO cell protein secretion, we predict that the elimination of unnecessary HCPs could have a non-negligible impact on protein production. We analyze the HCP content of 6-protein, 11-protein, and 14-protein knockout clones. These cell lines exhibit a substantial reduction in total HCP content (40%-70%). We also observe higher productivity and improved growth characteristics in specific clones. The reduced HCP content facilitates purification of a monoclonal antibody. Thus, substantial improvements can be made in protein titer and purity through large-scale HCP deletion, providing an avenue to increased quality and affordability of high-value biopharmaceuticals.

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Deciphering the determinants of recombinant protein yield across the human secretome

Project description:Mammalian cells are critical hosts for the production of most therapeutic proteins and many proteins for biomedical research. While cell line engineering and bioprocess optimization have yielded high protein titers of some recombinant proteins, many proteins remain difficult to express. Here we use systems biology methods to deciper the factors influencing yields in Chinese hamster ovary (CHO) cells as they produce proteins from the human secretome.

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