Volume 5 Supplement 1

The 4th Recombinant Protein Production Meeting: a comparative view on host physiology

Open Access

Expression of soluble and membrane proteins in E. coli

  • A James Link1,
  • Ki-Jun Jeong1 and
  • George Georgiou1
Microbial Cell Factories20065(Suppl 1):S15

DOI: 10.1186/1475-2859-5-S1-S15

Published: 10 October 2006

Our lab has developed a number of tools for enhancing the expression of soluble secreted protein as well as membrane proteins in bacteria. Specifically: (1) We have explored mutagenesis/screening and also host cell engineering strategies for the expression of mammalian and prokaryotic membrane proteins. This work has led to the development of simple approaches that can be used to obtain significantly increased yields of membrane proteins in E.coli. (2) Developed a high through strategy relying on flow cytometry for the isolation of mutant proteins exhibiting enhanced expression from combinatorial libraries. This latter technology has been used for the expression maturation of scFv and FAB antibody fragments.

Representative results illustrating the power of these methods will be discussed.

Authors’ Affiliations

(1)
Department of Chemical Engineering, Institute for Molecular and Cell Biology, University of Texas

Copyright

© Link et al; licensee BioMed Central Ltd. 2006

This article is published under license to BioMed Central Ltd.

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