A hemolysin secretion pathway-based novel secretory expression platform for efficient manufacturing of tag peptides and anti-microbial peptides in Escherichia coli

Abstract Background Although Escherichia coli has been widely used for the expression of exogenous proteins, secretory in this system is still a big obstacle. As one most important secretion pathways, hemolysin A (HlyA) E. can transport substrates directly from cytoplasm to extracellular medium without formation any periplasmic intermediate, making it an ideal candidate development production platform proteins. Results In work, we developed novel platform, THHly, based on HlyA system, and explored its applications efficient preparation quick detection tag peptides anti-microbial peptides. signal sequence fused C-terminal target peptide, with Tobacco Etch Virus (TEV) protease cleavage site 6*His between them. Five displayed good properties BL21 (DE3), among which T7 S were obtained by two rounds purification steps TEV cleavage, maintained their intrinsic immunogenicity. Furthermore, Cecropin Melittin, different types peptides, produced likewise verified possess anti-microbial/anti-tumor bioactivities. No significant bacterial growth inhibition was observed during fusion protein expression, indicating that form not only mediated but also decreased toxicity (AMPs) host bacteria. To best our knowledge, first report achieve these AMPs considerable potential manufacturing industrialization purposes. Conclusions The results demonstrate allowed thus suggesting promising strategy industrialized peptide pharmaceuticals or reagents. Graphical