We established three hybridomas (designated 2A12, 4C4 and 6H8) secreting monoclonal antibodies which react with N and H(heated) antigenic particles of poliovirus type 1 (Mahoney strain). One of these monoclonal antibodies, 4C4, had virus-neutralizing activity, while the other two were non-neutralizing. A solid-phase radioimmunoassay and a neutralization test indicated that the specificity of the neutralizing monoclonal antibody 4C4 was the same as that of the monospecific antibody HN31, previously prepared by us by absorbing poliovirus antiserum with an equine serum inhibitor-resistant mutant (M-HN31) of poliovirus. Furthermore, by means of immune electron microscopy, it was revealed that the combining site of the 4C4 neutralizing monoclonal antibody is on or around vertices of the N and H antigenic particles, while the other two monoclonal antibodies are directed to the entire surface of the antigens.


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