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• W2108241808 abstract "The Bacteriophage λ capsid protein gpD has been used extensively for fusion polypeptides that can be expressed from plasmids in Escherichia coli and remain soluble. In this study, a genetically controlled dual expression system for the display of enhanced green fluorescent protein (eGFP) was developed and characterized. Wild-type D protein (gpD) expression is encoded by λ Dam15 infecting phage particles, which can only produce a functional gpD protein when translated in amber suppressor strains of E. coli in the absence of complementing gpD from a plasmid. However, the isogenic suppressors vary dramatically in their ability to restore functional packaging to λDam15, imparting the first dimension of decorative control. In combination, the D-fusion protein, gpD::eGFP, was supplied in trans from a multicopy temperature-inducible expression plasmid, influencing D::eGFP expression and hence the availability of gpD::eGFP to complement for the Dam15 mutation and decorate viable phage progeny. Despite being the worst suppressor, maximal incorporation of gpD::eGFP into the λDam15 phage capsid was imparted by the SupD strain, conferring a gpDQ68S substitution, induced for plasmid expression of pD::eGFP. Differences in size, fluorescence and absolute protein decoration between phage preparations could be achieved by varying the temperature of and the suppressor host carrying the pD::eGFP plasmid. The effective preparation with these two variables provides a simple means by which to manage fusion decoration on the surface of phage λ." @default.
• W2108241808 created "2016-06-24" @default.
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• W2108241808 date "2013-05-03" @default.
• W2108241808 modified "2023-10-06" @default.
• W2108241808 title "Construction and analysis of a genetically tuneable lytic phage display system" @default.
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• W2108241808 doi "https://doi.org/10.1007/s00253-013-4898-6" @default.
• W2108241808 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3745828" @default.
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• W2108241808 hasPublicationYear "2013" @default.
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