Structural and antigenic variation of the structural protein VP3 in serotype 1 poliovirus isolated from vaccinees.
High resolution two-dimensional PAGE was used to analyse protein variation among serotype 1 poliovirus isolates. Viruses isolated from patients with recent histories of vaccination with live attenuated poliovirus were compared with prototype serotype 1 poliovaccine. The nonvaccine Mahoney and Brunenders strains of serotype 1 poliovirus were also analysed. The overall protein profile was conserved but the structural protein VP3 varied in its net charge among the viruses. Eight out of 14 clinical virus isolates had VP3 with a net basic charge identical to serotype 1 polio vaccine, whereas the remaining clinical isolates had an acidic VP3 similar to the nonvaccine type 1 strains. The altered VP3 mobility correlated with a change in antigenicity as determined by monoclonal antibodies directed to the neutralization site located on VP3. The data clearly illustrated the suitability of two-dimensional PAGE in analysing protein mutations in attenuated vaccine virus excreted by vaccinees.
Cash
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Department of Bacteriology, University of Aberdeen, Foresterhill, Scotland.
D000940:Antigenic Variation; D000956:Antigens, Viral / Q000032:analysis*; D002213:Capsid / Q000032:analysis* / Q000276:immunology; D036022:Capsid Proteins; D004591:Electrophoresis, Polyacrylamide Gel; D006367:HeLa Cells; D006801:Humans; D009500:Neutralization Tests; D017955:Poliovirus / Q000276:immunology*; D011055:Poliovirus Vaccine, Oral; D014611:Vaccination; D014764:Viral Proteins / Q000032:analysis*
D000956:Antigens, Viral; D036022:Capsid Proteins; D011055:Poliovirus Vaccine, Oral; C442542:VP3 protein, Poliovirus; D014764:Viral Proteins