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Article Abstract
Retrovirus-like particles (RVLPs) that are expressed during the production of monoclonal antibodies in Chinese hamster ovary (CHO) cell cultures must be removed during product recovery. Anion exchange chromatography (AEX) performed in product flow-through mode, a common component in the purification of monoclonal antibodies, has been shown to provide robust removal of a related retrovirus model, but it's ability to remove the actual RVLP impurities has not been directly investigated. We have determined the ability of a typical Q sepharose process to remove actual CHO RVLP impurities. Using small scale experiments with three model antibodies, we observe that this AEX process is capable of effectively removing both in-process and spiked RVLPs from different feedstocks containing different mAb products. In addition, we show that this AEX process also achieves a similarly high degree of RVLP removal during large scale manufacturing operations.
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View Article and Find Full Text PDFArticle Synopsis
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- Two specific retrovirus-like proteins, RTL8 and PEG10, work together to modulate the function of UBQLN2, enabling it to interact with PEG10 and play a role in stress granules during stress conditions.
- The research highlights how PEG10 affects the assembly and disassembly of stress granules and the presence of virus-like particles within them, revealing a novel connection between cellular protein management and retroviral elements.