Abstract
RECENT evidence suggests that the antiviral action of interferon is triggered by interaction with the cellular membrane. Mouse interferon covalently bound to Sepharose beads (IF-Sepharose) retains its antiviral potency and only direct contact with these particles produces the antiviral effect1,2. Preincubation of mouse L cells with Phaseolus vulgaris phytohaemagglutinin (PHA) blocks interferon action3. The inhibitory action of PHA can be almost completely reversed by washing PHA-treated cells with fetuin, a glycoprotein of high affinity for this plant lectin3. These data suggest that membrane sites interacting with interferon are carbohydrate-containing molecules that bind to PHA, although other explanations for the inhibitory action of PHA based on nonspecific steric or charge effects might be possible. To substantiate further that glycoside-containing membrane components bind to interferon, we have investigated the effect of gangliosides on interferon binding and action.
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BESANCON, F., ANKEL, H. Binding of interferon to gangliosides. Nature 252, 478–480 (1974). https://doi.org/10.1038/252478a0
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DOI: https://doi.org/10.1038/252478a0
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