Many biomedical applications require vectors that can direct the expression of multiple proteins; subunits of hetero-multimeric proteins, multiple therapeutic genes (combined and/or synergistic effects), or, simply, coexpression of a therapeutic protein along with proteins that act as (selectable) markers of transformed cells [ 1, 2].
Multiple therapeutic strategies were used, including protein-based inhibitors of the VEGF ligand or receptor binding, small molecule drugs targeting intracellular VEGFRs (e.g., VEGFR TKIs), vascular disrupting agents, as well as chemotherapy.
Among the multiple therapeutic strategies targeting the Bcl-2 protein family is the antagonism of the pro-survival function of anti-apoptotic proteins that seems to be the most attractive strategy.
Especially, protein aggregates could increase the immunogenicity of various therapeutic proteins, which might be explained by their multiple epitope character and/or to conformational changes of the aggregated protein molecules [14, 15, 17].
For many therapeutic proteins post-translational modifications, proteolytic processing and oligomerization of multiple chains are important for protein functionality, stability and efficient secretion.
These observations demonstrate the versatility of mT3 E. coli as a protein delivery system and suggest that it could be used for multiple therapeutic applications.
However, a non-allele-specific therapy in which both wild-type and mutant protein are suppressed is greatly preferred to avoid the challenges associated with regulatory approval of multiple therapeutic molecules (Sah and Aronin, 2011).
Roslin scientists are also working on a strain that can express therapeutic proteins in the whites of eggs.
But more fundamental changes, like adding therapeutic proteins to further speed healing, would require far more extensive testing.
