Absence of periplasmic DsbA oxidoreductase facilitates export of cysteine-containing passenger proteins to the Escherichia coli cell surface via the Igaβ autotransporter pathway
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Cited by (86)
Investigation of an AIDA-I based expression system for display of various affinity proteins on Escherichia coli
2024, Biochemical and Biophysical Research CommunicationsActivity control of autodisplayed proteins on the same outer membrane layer of E. coli by using Z-domain/streptavidin/and lipase/foldase systems
2017, Enzyme and Microbial TechnologyGoing beyond E. coli: autotransporter based surface display on alternative host organisms
2015, New BiotechnologyCitation Excerpt :Without the addition of this reducing agent, the autotransporter protein resided in the periplasm and was degraded by proteases located therein [55]. For surface translocation of cysteine-rich passengers, it was shown that it can be helpful to disable the periplasmic oxidoreductase DsbA, which is involved in disulphide bond formation [56]. As in the case of outer membrane proteases, analogous (or also homologous) enzymes have to be identified and possibly knocked out in new host organisms to enable the surface translocation of disulphide bond containing enzymes.
Type V secretion: From biogenesis to biotechnology
2014, Biochimica et Biophysica Acta - Molecular Cell ResearchSingle-cell characterization of autotransporter-mediated Escherichia coli surface display of disulfide bond-containing proteins
2012, Journal of Biological ChemistryExpression of active human P450 3A4 on the cell surface of Escherichia coli by Autodisplay
2012, Journal of BiotechnologyCitation Excerpt :Secondary structure analysis (TMpred program) of the CYP3A4 sequence suggested that the N-terminal part forms a transmembrane helix, which could interfere with the transport of the enzyme across the outer membrane. It could result in a periplasmic degradation of the passenger fusion protein as has been shown before for the Autodisplay passengers CtxB (Jose et al., 1996) and Aprotinin (Jose and Zangen, 2005). To overcome this possible limitation, the N-terminal 17 amino acids were deleted by a PCR based approach and the resulting truncated CYP3A4 autotransporter fusion protein was analyzed for transport and enzymatic activity as described above.
- 1
Present address: EVOTEC BioSystems GmbH, Grandweg 64, D-22529 Hamburg, Germany.
- 2
Present address: Mucos Pharma, Miraustrasse 17, D-13509 Berlin, Germany.