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New CHO Cells Study Results from University of Natural Resources and Applied Life Science Described (In search of expression bottlenecks in...

July 23, 2014



New CHO Cells Study Results from University of Natural Resources and Applied Life Science Described (In search of expression bottlenecks in recombinant CHO cell lines-a case study)

By a News Reporter-Staff News Editor at Biotech Week -- Investigators discuss new findings in CHO Cells. According to news reporting originating in Vienna, Austria, by NewsRx journalists, research stated, "The efficient production of recombinant proteins such as antibodies typically involves the screening of an extravagant number of clones in order to finally select a stable and high-producing cell line. Thereby, the underlying principles of a powerful protein machinery, but also potential expression limitations, often remain poorly understood."

The news reporters obtained a quote from the research from the University of Natural Resources and Applied Life Science, "To shed more light on this topic, we applied several different techniques to investigate a previously generated cell line (4B3-IgA), which expressed recombinant immunoglobulin A (IgA) with an unusually low specific productivity. Results were compared to the host cell line and to another recombinant CHO cell line (3D6-IgA) expressing another IgA that binds to an overlapping epitope. The low specific productivity of clone 4B3-IgA could not be explained by GCN or mRNA levels, but insufficiencies in protein maturation and/or secretion were determined. Despite the presence of free light chain polypeptides, they occasionally failed to associate with their heavy chain partners. Consequently, heavy chains were misassembled and accumulated to form intracellular aggregates, so-called Russell bodies. These protein deposits evoked the expression of increased amounts of ER-resident chaperones to combat the induced stress. Despite bottlenecks in protein processing, the cells' quality checkpoints remained intact, and predominantly correctly processed IgA was exported into the culture medium. The results of our study demonstrated that recombinant protein expression was impaired by heavy chain aggregation despite the presence of a disposable light chain and revealed elevated chaperone formation in combination with limited antibody assembly."

According to the news reporters, the research concluded: "Our studies suggest that the primary amino acid sequence and consequently the resulting structure of an expressed protein need to be considered as a factor influencing a cell's productivity."

For more information on this research see: In search of expression bottlenecks in recombinant CHO cell lines-a case study. Applied Microbiology and Biotechnology, 2014;98(13):5959-5965. Applied Microbiology and Biotechnology can be contacted at: Springer, 233 Spring St, New York, NY 10013, USA. (Springer - www.springer.com; Applied Microbiology and Biotechnology - www.springerlink.com/content/0175-7598/)

Our news correspondents report that additional information may be obtained by contacting D. Reinhart, Univ Nat Resources & Life Sci, Vienna Inst BioTechnol, Imaging Center, A-1190 Vienna, Austria. Additional authors for this research include W. Sommeregger, M. Debreczeny, E. Gludovacz and R. Kunert (see also CHO Cells).

Keywords for this news article include: Vienna, Europe, Austria, CHO Cells, Cell Line

Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC


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Source: Biotech Week


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