Influenza C virus contains a hemagglutinin and a receptor-destroying enzyme (RDE) whose specificities remain undetermined. In rat serum, there is a molecule that binds specifically to C virus, inhibiting its hemagglutinin. The complex between C virus and the rat serum inhibitor (RSI) was determined to be stable at 4 degrees C, but was disrupted within 20 to 90 min at 23 or 37 degrees C. Virus emerged from the complex with numerous functions intact, whereas the RSI at this point was inactivated, i.e., incapable of further inhibitory reactions with C virus. RSI could not be inactivated at these temperatures by nonviral components of allantoic fluid of infected chicken embryos; however, RSI inactivation was achieved by preparations of sucrose gradient-purified virus. Neutralization of viral hemagglutination activity with antiviral antibody protected the RSI from inactivation. RSI inactivation occurred at temperatures at which the viral RDE was active, and inhibition of viral RDE by periodate treatment sharply reduced the ability of virus to inactivate the RSI. One interpretation of the data suggests that RSI is a receptor analog reactive with both the hemagglutinin and RDE of C virus and that RSI inactivation is an assay of influenza C viral RDE.
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