Related Experiment Video
Updated: Jun 8, 2026

A Convenient and General Expression Platform for the Production of Secreted Proteins from Human Cells
Published on: July 31, 2012
Extracellular production of recombinant proteins using bacterial autotransporters
Wouter S P Jong1, Ana Saurí, Joen Luirink
1Section Molecular Microbiology, Department of Molecular Cell Biology, Faculty of Earth and Life Sciences, VU University, 1081 HV Amsterdam, Netherlands.
Abstract:
Escherichia coli is still a very popular host for the production of recombinant proteins at an analytical or industrial scale. Secretion of the proteins into the culture medium or display at the cell surface would be preferred in many applications but is hampered by the complex two-layered cell envelope. The autotransporter pathway is used by E. coli to secrete virulence factors via a relatively simple but efficient and specific mechanism. Here we discuss recent progress in the structural and mechanistic analysis of this pathway and the implications for future development of a versatile platform for secretion and display of heterologous proteins.
Related Concept Videos
Bacterial Translocation and Protein Secretion
Production of Pharmaceuticals
Upstream Processing
Gram-negative Bacterial Protein Secretion Systems
Overview of Protein Sorting and Transport
Protein sorting can be of two types: signal-based sorting and vesicle-based trafficking. In signal-based sorting, specific amino acid sequences called sorting signals target proteins to the proper location inside the cell either via gated transport or by protein translocation. In gated transport, folded...
Post-translational Translocation of Proteins to the RER
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...

