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Bac7 (1–35) is an Arg- and Pro-rich peptide antibiotic, produced in bovine cells to protect them from microbial infection. It has been demonstrated to inhibit the protein synthesis in  E. coli , leading to cell death. Because of its toxicity, no cost effective methods have been developed for Bac7 production in  Escherichia coli  for its potential clinical use. Here, we found a method to suppress Bac7 (1–35) toxicity in  E. coli  to establish its high expression system, in which Bac7 (1–35) was fused to the C-terminal end of protein S, a major spore-coat protein from Myxococcus xanthus, using a linker containing a Factor Xa cleavage site. The resulting His 6 -PrS 2 -Bac7 (1–35) (PrS 2  is consisted of two N-terminal half domains of protein S connected in tandem) was well expressed using the Single-Protein Production (SPP) system at low temperature and subsequently purified in a single step by using a Ni column. The combination of protein S fusion and its expression in the SPP system at low temperature appeared to suppress Bac7 (1–35) toxicity. Both the purified His 6 -PrS 2 -Bac7 (1–35) and His 6 -PrS 2 -Bac7 (1–35) treated by Factor Xa were proven to be a potent inhibitor for cell-free protein synthesis.

Suppression of the toxicity of Bac7 (1–35), a bovine peptide antibiotic, and its production in E. coli