ArticleMicrobial cell factories2012
Probing the applicability of autotransporter based surface display with the EstA autotransporter of Pseudomonas stutzeri A15.
Article in Microbial cell factories, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- A Novel Thermo-Alkaline Stable GDSL/SGNH Esterase with Broad Substrate Specificity from a Deep-Sea Pseudomonas sp.Marine biotechnology (New York, N.Y.) · 2024Article
- Comparing autotransporter β-domain configurations for their capacity to secrete heterologous proteins to the cell surface.PloS one · 2018Article
- Proof of concept for the simplified breakdown of cellulose by combining Pseudomonas putida strains with surface displayed thermophilic endocellulase, exocellulase and β-glucosidase.Microbial cell factories · 2016Article
- A nanobody:GFP bacterial platform that enables functional enzyme display and easy quantification of display capacity.Microbial cell factories · 2016Article
- BrkAutoDisplay: functional display of multiple exogenous proteins on the surface of Escherichia coli by using BrkA autotransporter.Microbial cell factories · 2015Article
- Decoration of outer membrane vesicles with multiple antigens by using an autotransporter approach.Applied and environmental microbiology · 2014Article
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Authors and funding
6 authors.
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Abstract
backgroundAutotransporters represent a widespread family of secreted proteins in Gram-negative bacteria. Their seemingly easy secretion mechanism and modular structure make them interesting candidates for cell surface display of heterologous proteins. The most widely applied host organism for this purpose is Escherichia coli. Pseudomonas stutzeri A15 is an interesting candidate host for environmentally relevant biotechnological applications. With the recently characterized P. stutzeri A15 EstA autotransporter at hand, all tools for developing a surface display system for environmental use are available. More general, this system could serve as a case-study to test the broad applicability of autotransporter based surface display.
resultsBased on the P. stutzeri A15 EstA autotransporter β-domain, a surface display expression module was constructed for use in P. stutzeri A15. Proof of concept of this module was presented by successful surface display of the original EstA passenger domain, which retained its full esterase activity. Almost all of the tested heterologous passenger domains however were not exposed at the cell surface of P. stutzeri A15, as assessed by whole cell proteinase K treatment. Only for a beta-lactamase protein, cell surface display in P. stutzeri A15 was comparable to presentation of the original EstA passenger domain. Development of expression modules based on the full-length EstA autotransporter did not resolve these problems.
conclusionsSince only one of the tested heterologous passenger proteins could be displayed at the cell surface of P. stutzeri A15 to a notable extent, our results indicate that the EstA autotransporter cannot be regarded as a broad spectrum cell surface display system in P. stutzeri A15.
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