Jossé, Lyne and Smales, C. Mark and Tuite, Mick F. (2012) Engineering the Chaperone Network of CHO Cells for Optimal Recombinant Protein Production and Authenticity. Methods in Molecular Biology, 824 (6). pp. 595-608. ISSN 1064-3745. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)
All proteins fold into a defined three-dimensional shape that is compatible with the cellular role and/or biological activity of those proteins. Molecular chaperones are a family of proteins whose role is to assist the folding and targeting of proteins in both normal and stressed cells. The rational manipulation of chaperone levels in a cell line engineered to produce a defined recombinant protein (rP) can significantly improve both the achievable steady-state levels and authenticity of a wide range of recombinant proteins. Here, we describe the methodology associated with expressing a variety of molecular chaperones in Chinese hamster ovary (CHO) lines in order to improve their recombinant protein production capacity. These chaperones include both those that facilitate the folding of the polypeptide chain (i.e. Hsp70, Hsp40) and those that can re-fold proteins that have misfolded in the cell (i.e. ClpB/Hsp104). This latter property is particularly important given the propensity for highly expressed recombinant proteins to misfold in the “foreign” cellular environment.
|Uncontrolled keywords:||Chinese hamster ovary cells - Molecular chaperone - Protein folding - Luciferase - Protein aggregation - Hsp104 - Hsp70 - Hsp40 - Recombinant antibody|
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||Sue Davies|
|Date Deposited:||27 Mar 2012 13:48|
|Last Modified:||09 Jun 2014 08:33|
|Resource URI:||https://kar.kent.ac.uk/id/eprint/29207 (The current URI for this page, for reference purposes)|