Secretion of recombinant proteins into the culture medium by Escherichia coli and Staphylococcus aureus.
The ability of staphylococcal protein A (SPA) to bind to the Fc part of IgG has been used for the purification of a number of heterologous gene products as fusion proteins. Both the SPA promoter and signal sequence function in Escherichia coli, as well as in a number of Gram-positive bacteria, which facilitates comparisons of the expressed specific products in different hosts. The expression system developed for E. coli yields excretion of the fusion protein to the growth medium, which makes E. coli a competitive alternative to Gram-positive bacteria for the expression of secreted products. The human peptide hormones insulin-like growth factors (IGF) I and II were expressed using the protein A system in E. coli and Staphylococcus aureus. Despite a high degree of structural homology, large differences in the yields were observed in the two hosts. This underlines the importance of investigating different bacterial hosts for a particular protein product.
Uhlén
M
M
Department of Biochemistry and Biotechnology, Royal Institute of Technology, Stockholm, Sweden.
Abrahmsén
L
L
D000595:Amino Acid Sequence; D003470:Culture Media; D004926:Escherichia coli / Q000378:metabolism*; D006728:Hormones / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D010957:Plasmids; D021382:Protein Sorting Signals / Q000032:analysis; D011994:Recombinant Proteins / Q000378:metabolism; D013205:Staphylococcal Protein A / Q000378:metabolism*; D013211:Staphylococcus aureus / Q000378:metabolism*
D003470:Culture Media; D006728:Hormones; D021382:Protein Sorting Signals; D011994:Recombinant Proteins; D013205:Staphylococcal Protein A