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Notably, fusing target proteins to a highly expressed bacterial protein has proven particularly effective for improving the expression level of membrane proteins in E. coli [21].
This study suggests a simple strategy for improving the expression and immunogenicity of HIV subtype-specific envelope antigens as plasmid or vector-borne immunogens.
This result suggests that incorporation of AT-rich codons can be utilized as a general strategy for improving the expression efficiency of a recombinant protein.
In this study, we evaluated codon context fitness as design criterion for improving the expression of thermostable invertase from Thermotoga maritima in Escherichia coli and explored the relevance of secondary structure regions for folding and expression.
Codon harmonization may further provide a general strategy for improving the expression of soluble functional proteins during heterologous expression in hosts other than E. coli.
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The information generated in this work describes a novel phenomenon and is useful for designing rational infection strategies needed in several applications for improving the simultaneous expression of two recombinant proteins in systems based on viral gene delivery.
Revealing general mechanisms that control gene expression is important for understanding normal and pathological cell functions and for improving the design of expression systems.
These data were evaluated with the aim of generating new hypotheses for improving the micropropagation protocol using the expression of specific genes as physiological markers.
Though a bacterial thioesterase from Streptococcus pyogenes was employed for improving the fatty acid synthesis, expression of this thioesterase in E. coli only obtained 1.3-fold more total fatty acids than the wild-type E. coli, still with C16 and C18 fatty acids as its major components [ 17].
"Rescuing" transgene expression by co-integration may provide a general solution for improving the efficiency of heterologous gene expression in transgenic animals.
The use of this promoter for high level protein expression under hypothermic condition therefore demonstrates an attractive alternative in production techniques since it combines both, a novel genetic construct that is directly linked to the individual process conditions with the potential for improving the performance also for other mammalian expression systems.
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