원문정보
초록
영어
Extracellular production of recombinant proteins in E. coli has received considerable attention due to its significant advantages over cytoplasmic or periplasmic production. However, efficient secretion of recombinant proteins into the culture medium of E. coli remains a challenge due to the intrinsic limitations of the secretion machinery. Here we report a systematic proteome-based
approach for high-level extracellular production of recombinant proteins. First, the extracellular proteome of an E. coli B strain was analyzed to identify motifs as potential fusion partners. Next, we expressed each open reading frame of the selected motifs and determined the protein profiles of the culture medium. The highest secreting motif was used as the carrier protein to produce several "passenger proteins" in the culture medium. Those model passenger proteins
show a wide versatility with respect to the proteins' length and origin. In addition, the polypeptides accumulated in the medium at high concentrations ranging from 15 to 500 mg/L. These findings demonstrate a proteome-based approach for high-level production of recombinant proteins in the culture medium of E. coli.