Knockout of a difficult-to-remove CHO host cell protein, lipoprotein lipase, for improved polysorbate stability in monoclonal antibody formulations.

摘要: While the majority of host cell protein (HCP) impurities are effectively removed in typical downstream purification processes, a small population HCPs particularly challenging. Previous studies have identified that challenging for variety reasons. Lipoprotein lipase (LPL)-a Chinese hamster ovary (CHO) HCP functions to hydrolyze esters triglycerides-was one ten previous as being susceptible retention processing. LPL may degrade polysorbate 80 (PS-80) and 20 (PS-20) final product formulations due structural similarity between polysorbates triglycerides. In this work, recombinant was found enzymatic activity against PS-80 PS-20 range solution conditions mAb formulations. knockout CHO cells were created with CRISPR TALEN technologies resulting culture harvest fluid demonstrated significantly reduced degradation without significant impact on viability when compared wild-type samples. Biotechnol. Bioeng. 2017;114: 1006-1015. © 2016 Wiley Periodicals, Inc.