Effects of anionic and nonionic polymers on fusion and binding of Sendai virus to human erythrocyte ghosts

Effects of various polymers (dextran sulfate, dextran and polyethylene glycol) on binding and fusion of Sendai virus to target cells were studied by use of fluorescence spectroscopy. Direct binding of dextran sulfate but not dextran to Sendai virus was detected. Anionic and nonionic polymers showed definite effects on segmental motions of the viral envelope proteins. Sendai virus binding to human erythrocyte ghost membranes (HEG) was reduced by dextran sulfate and dextran while the fusion temperature dependence remained unaltered at approximately 20 degrees C. Nonionic polymer, polyethylene glycol, caused an increase in extent of fusion of Sendai virus with HEG. Segmental motion of viral envelope proteins, determined in terms of anisotropy of fluorescent probes attached to viral surface proteins, exhibited a temperature dependent transition at 20 degrees C by a sharp change from restricted to less restricted motion. In the presence of each of the polymers, this transition was no longer apparent. Since fusion did occur in the presence of all polymers, the temperature dependent characteristic of Sendai virus target cell fusion can be said not to depend on viral surface protein segmental motion. A reasonable and coherent explanation was given for the apparent disparity between the effects of inhibiting and enhancing polymers on fusion and motion of viral proteins.