A panel of mouse hybridomas secreting monoclonal antibody to serum hepatitis Be antigen (HBeAg) was produced from mice immunized with denatured hepatitis B core antigen (HBcAg). This panel could be divided broadly into two groups. Within each group, the monoclonal antibodies recognized a single antigenic site, designated either e-α or e-β, and generally exhibited a high degree of cross-inhibition. In contrast, between the two groups of antibodies there was little or no cross-inhibition. The antigens of serum HBeAg and denatured HBcAg appeared to be very similar. Both behaved as molecules carrying only a single e-α or e-β site, in spite of native serum HBeAg having an apparent molecular weight of 300000. It is inferred that e-α and e-β sites may be involved in the polymerization of HBeAg into HBcAg and that during this process mutual masking of antigenic sites may occur.

Keyword(s): HBeAg to HBcAg conversion , HBV and MAb

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