A generalised module for the selective extracellular accumulation of recombinant proteins.
BACKGROUND
It is widely believed that laboratory strains of Escherichia coli, including those used for industrial production of proteins, do not secrete proteins to the extracellular milieu.


RESULTS
Here, we report the development of a generalised module, based on an E. coli autotransporter secretion system, for the production of extracellular recombinant proteins. We demonstrate that a wide variety of structurally diverse proteins can be secreted as soluble proteins when linked to the autotransporter module. Yields were comparable to those achieved with other bacterial secretion systems.


CONCLUSIONS
The advantage of this module is that it relies on a relatively simple and easily manipulated secretion system, exhibits no apparent limitation to the size of the secreted protein and can deliver proteins to the extracellular environment at levels of purity and yields sufficient for many biotechnological applications.
School of Immunity and Infection, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom.
Yanina R
YR
Sevastsyanovich
Denisse L
DL
Leyton
Timothy J
TJ
Wells
Catherine A
CA
Wardius
Karina
K
Tveen-Jensen
Faye C
FC
Morris
Timothy J
TJ
Knowles
Adam F
AF
Cunningham
Jeffrey A
JA
Cole
Ian R
IR
Henderson
D058947:Bacterial Secretion Systems; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D005110:Extracellular Space / Q000235:genetics / Q000378:metabolism*; D021381:Protein Transport; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism*
D058947:Bacterial Secretion Systems; D011994:Recombinant Proteins