A generalised module for the selective extracellular accumulation of recombinant proteins

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. Here, we report the development of a generalised module, based on an E. coli autotransporter secretion system, for the p...

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Bibliographic Details
Published in:Microbial cell factories 2012-05, Vol.11 (1), p.69-69, Article 69
Main Authors: Sevastsyanovich, Yanina R, Leyton, Denisse L, Wells, Timothy J, Wardius, Catherine A, Tveen-Jensen, Karina, Morris, Faye C, Knowles, Timothy J, Cunningham, Adam F, Cole, Jeffrey A, Henderson, Ian R
Format: Article
Language:English
Subjects:
Autotransporter
Bacterial Secretion Systems
Bacteriology
Enzymes
Escherhichia coli
Escherichia coli
Escherichia coli - genetics
Escherichia coli - metabolism
Extracellular Space - genetics
Extracellular Space - metabolism
Methods
Microbiological synthesis
Microbiology
Physiological aspects
Protein Transport
Proteins
Recombinant protein production
Recombinant proteins
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Secretion
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Summary: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. 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. 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.
ISSN:1475-2859
1475-2859
DOI:10.1186/1475-2859-11-69