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Secretion of heterologous proteins into  Escherichia coli  cell culture medium offers significant advantages for downstream processing over production as inclusion bodies; including cost and time savings, and reduction of endotoxin. Signal peptides play an important role in targeting proteins for translocation across the cytoplasmic membrane to the periplasmic space and release into culture medium during the secretion process. Alpha toxin H35L  (AT H35L ) was selected as an antigen for vaccine development against  Staphylococcus aureus  infections. It was successfully secreted into culture medium of  E. coli  by using bacterial signal peptides linked to the N-terminus of the protein. In order to improve the level of secreted AT H35L , we designed a series of novel signal peptides by swapping individual domains of modifying dsbA and pelB signal peptides and tested them in a fed-batch fermentation process. The data showed that some of the modified signal peptides improved the secretion efficiency of AT H35L  compared with  E. coli  signal peptides from dsbA, pelB and phoA proteins. Indeed, one of the novel signal peptides improved the yield of secreted AT H35L  by 3.5-fold in a fed-batch fermentation process and at the same time maintained processing at the expected site for signal peptide cleavage. Potentially, these new novel signal peptides can be used to improve the secretion efficiency of other heterologous proteins in  E. coli . Furthermore, analysis of the synthetic signal peptide amino acid sequences provides some insight into the sequence features within the signal peptide that influence secretion efficiency.   Electronic supplementary material  The online version of this article (doi:10.1186/s13568-017-0394-1) contains supplementary material, which is available to authorized users.

Novel signal peptides improve the secretion of recombinant Staphylococcus aureus Alpha toxinH35L in Escherichia coli