Susmita Chaudhuri, Priyanka Maurya, Manpreet Kaur, Ashutosh Tiwari, Nicole Borth, Shinjini Bhatnagar and Niraj Kumar
The demand for recombinant protein therapeutics is increasing worldwide and hence improvements in the overall yield of such products from bioprocess are of great interest to make them affordable. Chinese Hamster Ovary (CHO) cells are the most commonly used cell lines for large scale production of such high-quality (human-like) recombinant protein products. Typically, product is released, along other secretory proteins, by the cell into the culture media. These secreted proteins may have significant impact on cell growth, product quality & quantity during the production culture and the designing of strategies for efficient product purification. However, only few efforts have been made to date to explore these secreted proteins (the “secretome”), although significant technological advancements have been witnessed in the field of proteomics during the last two decades. Even from these, the majority of studies have identified a high proportion of intracellular- and non-secretory proteins in culture supernatants which could be possibly due to the unavailability of well-defined methodologies for sample collection & preparation for massspectrometry and/or followed data analysis using databases that contain less number of secretory proteins. As a result, secreted CHO proteins and their potential in regulation of recombinant protein production remain unexplored.
Therefore, the goal of this article is to provide an overview of the importance of secreted proteins in improving recombinant protein production from bioprocesses and to outline potential ways for their efficient investigation using proteomic approaches. This knowledge could help in increasing the overall yield from production processes.
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