Mild treatment of chick embryo and L cells with proteases resulted in decreased induction by poly(rI).poly(rC) of interferon and of antiviral resistance, as well as in reduced uptake of [H]-poly(rI).poly(rC). The enzyme treatment of the cells neither significantly affected their sensitivity to exogenous interferon nor suppressed interferon induction by a virus inducer. The supernatant fluid from the trypsintreated cells contained a substance which complexed with poly(rI).poly(rC), resulting in inhibition, but not in irreversible inactivation, of its interferon-inducing ability. The induction was also inhibited when the cells were first incubated with the inducer and then treated with trypsin. Since trypsin presumably acts primarily on the cell surface, these results are interpreted to indicate that the binding of poly(rI).poly(rC) to cell surface sites and its persistence at the surface for a certain period of time plays an essential role in interferon induction.


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