Partial fusion activity of influenza virus toward liposomes and erythrocyte ghosts is distinct from viral inactivation.

Final extents of fusion of influenza virus (A/PR/8/34 strain) with neutral and partially acidic liposomes were monitored with (i) a fluorescence resonance energy-transfer assay in which the liposomes were labeled and (ii) by the dequenching of octadecylrhodamine, initially incorporated in the viral membrane. The latter assay was also employed in the fusion of influenza virus and Sendai virus with erythrocyte ghosts. In all cases, a phenomenon of partial fusion activity of the virus was observed, which is distinct from low pH inactivation. The unfused influenza or Sendai virions, which were separated by sucrose gradient centrifugation from liposomes or erythrocyte ghosts exhibited again partial fusion activity toward freshly added liposomes or ghosts, respectively. The conclusion is that the fraction of initially bound and unfused virions does not consist of defective particles, but rather of particles bound to the target membranes via inactive sites on the virus (or on cellular membranes), or else, partial fusion activity is a manifestation of a certain probability of production of fusion inactive sites by irreversible association of viral glycoproteins or peptides in the target membrane.