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Epitope evolution in poliovirus maturation.

B Rombaut, R Vrijsen, A Boeyé

    Archives of Virology
    |January 1, 1983
    PubMed
    Summary
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    Monoclonal antibodies reveal distinct poliovirus epitopes. Native poliovirus antigen has two epitopes (N1, N2), with only N1 on 14S particles, while heated poliovirus antigen exposes a different epitope (H).

    Area of Science:

    • Virology
    • Immunology
    • Structural Biology

    Background:

    • Poliovirus structure and antigenicity are crucial for vaccine development and understanding viral infection.
    • Monoclonal antibodies are key tools for characterizing viral epitopes.

    Purpose of the Study:

    • To investigate the distinct epitopes present on native (N) and heated (H) poliovirus particles.
    • To characterize the antigenic differences between empty capsids and 14S poliovirus particles.

    Main Methods:

    • Utilized eight monoclonal antibodies specific for native poliovirus antigen.
    • Analyzed the reactivity of these antibodies with empty capsids and 14S poliovirus particles.
    • Investigated the effect of infected cell extract-catalyzed polymerization on poliovirus epitopes.

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    Main Results:

    • All eight monoclonal antibodies recognized native epitopes on empty capsids.
    • Only three of these antibodies recognized epitopes on 14S particles, suggesting the presence of distinct N1 and N2 epitopes.
    • A separate epitope (H) on 14S particles was identified using antibodies to heated poliovirus antigen.
    • Polymerization of 14S particles resulted in empty capsids primarily expressing N1 and N2 epitopes, lacking the H epitope.

    Conclusions:

    • Poliovirus possesses at least two distinct native epitopes (N1 and N2), with N1 being present on 14S particles.
    • A distinct heated epitope (H) is also present on 14S particles.
    • These findings clarify the antigenic composition of different poliovirus particle types and inform vaccine design.