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High levels of circulating neutralizing antibody in normal animals to recombinant mouse interferon-beta produced in yeast.

Plasma from normal outbred Swiss mice not previously given interferon (IFN) neutralized a glycosylated (high-mannose) recombinant murine IFN-beta made in yeast (rMuIFN-beta y). The neutralization antibody titers were as high as 1:6,000 versus rMuIFN-beta y, whereas the titers obtained with native murine IFN-beta (MuIFN-beta) were 100-fold less; a recombinant murine IFN-beta make in Escherichia coli (rMuIFN-beta ec) was not neutralized at 1:10 dilution of plasma. An ELISA using rMuIFN-beta y demonstrated that it is gamma immunoglobulins in normal mouse plasma that bind rMuIFN-beta y. Normal rabbit serum also had very high endogenous neutralizing activity (1:5,300) against rMuIFN-beta y. Significant neutralizing activity also was detected in newborn bovine and normal human serum as well as pooled human immune serum globulin. Thus, endogenous neutralizing activity directed presumably at the carbohydrate residues of highly glycosylated recombinant proteins produced in yeast may limit their clinical utility.