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Analysis of IgG1 producing CHO cells

ABSTRACT: The effects of changes in bioprocessing parameters (temp, pH, DO) on anti-IL8 IgG1 producing Chinese hamster ovary (CHO) cells were studied on the level of host cell proteome expression using TMT-SPS-MS3.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Cricetulus Griseus (chinese Hamster) (cricetulus Barabensis Griseus)

TISSUE(S): Cell Culture

SUBMITTER: Lisa Strasser

LAB HEAD: Jonathan Bones

PROVIDER: PXD017779 | Pride | 2021-04-09

REPOSITORIES: Pride

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			Action	DRS
	2016_04221_NIBRT_1ug_SetA_001_160426205711.raw	Raw
	2016_04221_NIBRT_1ug_SetA_002.raw	Raw
	2016_04221_NIBRT_1ug_SetA_003.raw	Raw
	2016_04221_NIBRT_1ug_SetA_004.raw	Raw
	2016_04221_NIBRT_1ug_SetA_005.raw	Raw

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Publications

Proteomic Profiling of IgG1 Producing CHO Cells Using LC/LC-SPS-MS<sup>3</sup>: The Effects of Bioprocessing Conditions on Productivity and Product Quality.

Strasser Lisa L Farrell Amy A Ho Jenny T C JTC Scheffler Kai K Cook Ken K Pankert Patrick P Mowlds Peter P Viner Rosa R Karger Barry L BL Bones Jonathan J

Frontiers in bioengineering and biotechnology 20210409

The biopharmaceutical market is dominated by monoclonal antibodies, the majority of which are produced in Chinese hamster ovary (CHO) cell lines. Intense cell engineering, in combination with optimization of various process parameters results in increasing product titers. To enable further improvements in manufacturing processes, detailed information about how certain parameters affect cellular mechanisms in the production cells, and thereby also the expressed drug substance, is required. Theref ...[more]

PMID: 33898396

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Quantitative analysis of the supernatant from native and transfected CHO cells using iTRAQ 8-plex technique

Project description:We employed UPLC-MS/MS with iTRAQ 8-plex labeling to quantitatively analyze the supernatant produced by two Chinese hamster ovary (CHO) cell lines (CHO K1SV and CHO CAT-S). In each case, the supernatant from the host and three transfected clones were analyzed at days 5, 7, and 10 of culture. A total of eight iTRAQ 8-plex experiments were performed.

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Hyperosmolality in CHO Culture: Effects on Proteome

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2022-05-20 | PXD027443 | Pride

Exoproteome in a perfusion bioreactor containing antibody-producing CHO cells at various cell densities

Project description:Chinese Hamster ovary (CHO) cells are the main platform used to produce recombinant proteins in the biopharmaceutical industry and are commonly cultured in either fed-batch or perfusion mode. However, the optimization of the complex biological systems used in such processes is extremely challenging. Omics approaches can reveal otherwise unknown characteristics of these systems and identify culture parameters that can be manipulated to optimize the cultivation process. Here we have applied proteomic profiling to a monoclonal antibody (mAb) production operated in perfusion mode to explore how cell biology and reactor environment change as the cell density reaches ≥ 200 x 106 cells/mL. The proteomics data show an increase of structural proteins as cell density increase, signs of oxidative stress and changes in glutathione metabolism at very high cell densities. Additionally, metabolomic profiling was carried out. See article “High cell density culture has a maintained exoproteome and metabolome” for more information.

2018-07-04 | PXD008760 | Pride

Isolation and Characterization of small EVs from CHO-K1 cell cultures

Project description:Chinese hamster ovary (CHO) cells are widely used host cells for recombinant protein production and currently the most commonly utilized mammalian organism in large scale biopharmaceutical production. Since the discovery of exosomes as a new type of small extracellular vesicles (EVs) by Johnstone et al., interest in EV research greatly increased in recent years. However, they yet pose a blank space in CHO research. Exosomes are 30 – 150 nm small vesicles, that derive from the endosomal network and can therefore be distinguished from plasma membrane-shed microvesicles (100 – 1000 nm in diameter) and apoptotic vesicles (50 – 5000 nm), which are secluded over the course of programmed cell death. It turned out exosomes are not only vehicles of cellular waste disposal, as was initially assumed, but also a conserved mechanism of cellular communication. This work aims to outline possible separation techniques followed by a differential proteomic and transcriptomic characterization of CHO EVs over the course of a bioreactor batch cultivation. Therefore, a protocol yielding sEVs with a strong exosomal marker enrichment is compared with HCP, lEVs and whole cell lysate (WCL) from the same batch process. This may allow for further studies in this field to have reference data for evaluation of exosome isolation techniques, separation purity and CHO EV composition in general.

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Chinese Hamster Ovary cell proteins co-purified with recombinant HIV-1 envelopes, part 2

2017-09-04 | PXD006061 | Pride

Chinese Hamster Ovary cell proteins co-purified with recombinant HIV-1 envelopes, part 4

2017-09-04 | PXD006063 | Pride

Chinese Hamster Ovary cell proteins co-purified with recombinant HIV-1 envelopes, part 3

2017-09-04 | PXD006062 | Pride

Spatial proteomics reveals differences in the cellular architecture of antibody-producing CHO and plasma-cell derived cells

Project description:Most of the recombinant biotherapeutics employed today to combat severe illnesses e.g. various types of cancer or autoimmune diseases are produced by Chinese hamster ovary (CHO) cells. To meet the growing demand of these pharmaceuticals, CHO cells are under constant development in order to enhance their stability and productivity. The last decades saw a shift from empirical cell line optimization towards rational cell engineering using a growing number of large omics datasets to alter cell physiology on various levels. Especially proteomics workflows reached new levels in proteome coverage and data quality due to advances in high-resolution mass spectrometry instrumentation. One type of workflow concentrates on spatial proteomics by usage of subcellular fractionation of organelles with subsequent shotgun mass spectrometry proteomics and machine learning algorithms to determine the subcellular localization of large portions of the cellular proteome at a given time. Here, we present the first subcellular spatial proteome of a CHO-K1 cell line producing high titers of recombinant antibody and comparison to the spatial proteome of an antibody-producing plasma cell-derived (PCD) myeloma cell line. Both cell lines show strong correlation of immunoglobulin G chains with chaperones and proteins associated in protein glycosylation within the endoplasmic reticulum compartment. However, we report differences in the localization of proteins associated to vesicle-mediated transport, transcription and translation, which may affect antibody production in both cell lines. Furthermore, pairing subcellular localization data with protein expression data revealed elevated protein masses for organelles in the secretory pathway in MPC-11 cells. Our study highlights the potential of subcellular spatial proteomics combined with protein expression as potent workflow to identify characteristics of highly efficient recombinant protein expressing cell lines.

2022-08-02 | PXD029115 | Pride

Mechanistic insights into the biological activity of S-Sulfocysteine in CHO cells using a multi-omics approach

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