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Rapid prediction of expression and refolding yields using phage display

Abstract

Aggregation limits the recombinant production of many commercially important proteins. We have recently identified mutations that control the aggregation behavior of human antibody variable domains (Dudgeon K., Rouet R., Kokmeijer I., Schofield P., Stolp J., Langley D., Stock D. and Christ D. (2012) Proc Natl Acad Sci USA, 109, 10879-10884. This has allowed the generation of a panel of human antibody variable heavy domains with a defined range of aggregation propensities. Here we utilize this unique resource to validate a previously reported heat-denaturation method on phage (Jespers L., Schon O., Famm K. and Winter G. (2004) Nat Biotechnol, 22, 1161-1165. Our experiments revealed that the method is not only robust in respect to denaturation conditions on phage, but also highly indicative of solution behavior. In particular, it is an excellent predictor of expression and refolding yields.

Type Journal
Authors Dudgeon, K.; Rouet, R.; Christ, D.
Responsible Garvan Author
Publisher Name PROTEIN ENGINEERING DESIGN & SELECTION
Published Date 2013-10-01
Published Volume 26
Published Issue 10
Published Pages 671-4
Status Published in-print
DOI 10.1093/protein/gzt019
URL link to publisher's version http://www.ncbi.nlm.nih.gov/pubmed/23690626
OpenAccess link to author's accepted manuscript version https://publications.gimr.garvan.org.au/open-access/11800