High-Level Expression of a Bioengineered, Cysteine-Free Hepatocyte-Stimulating Factor (Interleukin 6)-Like Protein

Hepatocyte-stimulating factor, interferon-β 2, B-cell stimulation factor 2, and hybridoma/plasmacytoma growth factor are identical proteins presently referred to as interleukin 6 (IL-6). Through the use of synthetic oligonucleotide technology, we have constructed a biologically active recombinant IL...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1988-12, Vol.85 (24), p.9426-9430
Main Authors: Jambou, Robert C., Snouwaert, John N., Bishop, Gail Abendroth, Stebbins, John R., Frelinger, Jeffrey A., Fowlkes, Dana M.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Animals
Antiviral Agents
B lymphocytes
B-Lymphocytes - drug effects
Base Sequence
Biological and medical sciences
Biotechnology
Cell lines
Cysteine
Escherichia coli - genetics
Fundamental and applied biological sciences. Psychology
Genetic engineering
Genetic technics
Genetic vectors
Health. Pharmaceutical industry
Hepatocytes
Humans
Industrial applications and implications. Economical aspects
Interleukin-6
Interleukins - analysis
Interleukins - genetics
Interleukins - pharmacology
Liver - drug effects
Methods. Procedures. Technologies
Molecular Sequence Data
Nucleotides
Oligonucleotides
Other active biomolecules
Production of active biomolecules
Proteins
Quaternary ammonium compounds
Rats
Recombinant Proteins - analysis
Sulfates
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Summary:Hepatocyte-stimulating factor, interferon-β 2, B-cell stimulation factor 2, and hybridoma/plasmacytoma growth factor are identical proteins presently referred to as interleukin 6 (IL-6). Through the use of synthetic oligonucleotide technology, we have constructed a biologically active recombinant IL-6 (rIL-6) gene based on the sequence of a human IL-6 cDNA. The synthetic gene encodes a cysteine-free, bioengineered rIL-6 protein that is expressed at high levels in Escherichia coli as a tripartite fusion protein. Cleavage of the fusion protein with collagenase releases a 23-kDa rIL-6 protein that can be easily purified to homogeneity. We show that the rIL-6 protein displays a range of biological activities similar to those of natural human IL-6, as demonstrated by its ability to (i) protect cells from viral infection, (ii) stimulate the synthesis of fibrinogen in rat FAZA 967 cells, and (iii) induce the terminal differentiation of B cells, resulting in elevated secretion of immunoglobulin.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.85.24.9426