The glycoprotein nature of murine gamma interferon

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Abstract
Synthesis of murine gamma interferon (MuIFNγ) by phytohemagglutinin (PHA)-stimulated spleen cells was inhibited in a dose-dependent manner by graded concentrations of tunicamycin or 2-deoxy-glucose, both of which inhibit glycosylation. The homologous (murine) and heterologous (rat) antiviral activities of the MuIFNγ preparations secreted in the presence of the various concentrations of either glycosylation inhibitor were reduced to similar degrees. MuIFNγ synthesized in the presence of tunicamycin (tunicamycin-MuIFNγ) exhibited a lower molecular weight (MW), a lack of binding to immobilized Concanavalin-A (Con A), and different charge properties when compared to MuIFNγ produced in absence of inhibitor (control-MuIFNγ). Potent rabbit and rat neutralizing antibodies raised against a control-MuIFNγ subcomponent, isolated by its specific binding to a Con A affinity column, neutralized the antiviral activity of tunicamycin-MuIFNγ to the same degree as the immunogen.