High-level expression of a bioengineered, cysteine-free hepatocyte-stimulating factor (interleukin 6)-like protein

R. C. Jambou, J. N. Snouwaert, G. A. Bishop, J. R. Stebbins, J. A. Frelinger, D. M. Fowlkes

Research output: Contribution to journalArticle

40 Scopus citations

Abstract

Hepatocyte-stimulating factor, interferon-β2, 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.

Original languageEnglish (US)
Pages (from-to)9426-9430
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume85
Issue number24
DOIs
StatePublished - 1988

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