Demonstrates high-level, temperature-regulated synthesis of biologically active human fibroblast interferon in E. coli, though it inhibits host growth.
High-yield E. coli expression of active human interferon is feasible; leaves open optimization to mitigate host-growth inhibition before scalable therapeutic use.
We have obtained high level synthesis in Escherichia coli of mature human fibroblast interferon using a plasmid vector that was designed to allow easy coupling of a DNA coding region to the initiator AUG of the replicase gene of the RNA phage MS2 cloned downstream of phage lambda's leftward promoter. The activity of the promoter can be regulated by temperature. Induced cells accumulated the interferon up to 4% of the total cellular protein. The biological activity of the product amounted to 4 X 10(9) international units per litre of culture. The synthesis of human fibroblast interferon was shown to drastically inhibit the growth rate of the bacterial host.
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Remaut et al. (1983) studied this question.
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