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Volume 271, Number 39, Issue of September 27, 1996 pp. 23902-23906
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Partial Fusion Activity of Influenza Virus toward Liposomes and Erythrocyte Ghosts Is Distinct from Viral Inactivation

(Received for publication, January 31, 1996, and in revised form, June 7, 1996)

João Ramalho-Santos ^§ , Maria C. Pedroso de Lima ^¶ and Shlomo Nir

From the  Center for Neurosciences of Coimbra, ^§ Department of Zoology, and ^¶ Department of Biochemistry, University of Coimbra, 3000 Coimbra, Portugal and the  Faculty of Agriculture, Seagram Centre for Soil and Water Sciences, Hebrew University of Jerusalem, 76100 Rehovot, Israel

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.

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