Neutralization of poliovirus by polyclonal antibodies requires binding of a single IgG molecule per virion.

Neutralization of poliovirus type 1 was studied using radioactively labelled polyclonal IgG. With nonsaturating antibody concentrations various virus-antibody complexes were produced which were isolated by sucrose gradient centrifugation and identified by electron microscopy as virus monomers, dimers, trimers, tetramers and pentamers. The neutralization rate (n.r.) of each of the virus-antibody complexes relative to non-neutralized virus and the stoichiometry have been estimated. The monomer fraction showed that about every fifth virion was associated with one IgG molecule and neutralized. The antibody was bivalently attached. The majority of virus particles formed aggregates of different sizes, which were cross-linked by antibodies. The following neutralization rates and ratios of IgG to virus (IgG/V) were determined for the oligomers: dimers, 59.2 per cent n.r. and 0.55 IgG/V; trimers, 67.3 per cent n.r. and 0.66 IgG/V; tetramers, 79.0 per cent n.r. and 0.75 IgG/V; pentamers, 86.3 per cent n.r. and 0.98 IgG/V. Two different mechanisms of neutralization are proposed: i) an antibody-mediated mechanism specifically inhibits infectivity of the monomer virus-antibody complexes and ii) reduction of infectivity of oligomer virus-antibody complexes is caused simply by reduction of the actual number of infectious units. Immunoprecipitation of the denatured capsid proteins showed that only VP 1 was recognized by the polyclonal IgGs.