ABSTRACT
Post-translational modification is a chemical alteration, enabling to escape from nature’s limited genetic confinement. As a vital source of protein diversity, post-translational modification confers extended protein function by covalently attaching chemical groups to the specific and selected residue in a protein. Numerous approaches have been applied to fabricate authentic heterologous proteins with post-translational processes for the functional and structural studies as well as therapeutic application. The domesticated Silkworm Bombyx mori, recognized as a natural bioreactor to produce silk, is an emerging reliable host for eukaryotic protein production with fail-safe post-translational modification. This chapter discusses three post-translational modifications including phosphorylation, biotinylation and disulfide bond formation implemented in heterologous proteins produced in silkworm Bombyx mori nucleopolyhedrovirus (BmNPV) bacmid-based expression system. These recombinant proteins are human acetyl-CoA carboxylase and malonyl-CoA carboxylase, critical metabolic enzymes for anabolic and catabolic lipid metabolism, and porcine insulin-like peptide 3, a member of relaxin/insulin superfamily, and all of these are very refractory to produce. The critical assessment of post-translational modification demonstrates that the silkworm expression modality is a reliable eukaryotic protein production platform equipped with unfailing post-translational phosphorylation, biotinylation and disulfide bond formation.
