Interactions between hepatitis B virus and polymeric human albumin I. Production of monoclonal anti‐idiotypes (anti‐anti‐polymeric human albumin) which recognize hepatitis B virus surface antigen

Abstract

In an attempt to characterize the polymeric human albumin (polyHSA) receptor expressed on hepatitis B virus and hepatocytes, we have used a human anti-polyHSA IgG to generate monoclonal anti-idiotypes (anti-Id) which bear the internal image of polyHSA and mimic its binding activity. Two monoclonal anti-Id antibodies, 63.14 and 70.F9, were strongly reactive in both radioimmunoassay and enzyme-linked immunosorbent assay (ELISA) with the F(ab')2 of the immunogen as well as with purified hepatitis B surface antigen (HBsAg) expressing various subtypes. The specificity of the binding of anti-Id to HBsAg was confirmed in direct ELISA and by Western blot analysis. These experiments also showed that the anti-Id bind to a site expressed on the major 24-kDa protein of HBsAg particles, and that this recognition is specifically inhibited by polyHSA. Experiments on cellular staining and radioimmunoprecipitation on HBsAg-positive and -negative cell lines showed that the anti-Id recognize intracellular HBsAg but not other liver cell proteins, including the putative polyHSA receptor. These data indicate, therefore, that the monoclonal anti-Id mimic the binding activity of polyHSA and recognize its binding site on the virus. The inability of both anti-Id to react with the hepatocyte surface suggests either the absence of a specific hepatic polyHSA receptor or the expression of one with a different configuration.

Monoclonal anti-idiotypic antibodies regulate the expression of virus-induced murine myocarditis

“…Anti-ld88 binding was assessed by using a peroxidase-conjugated goat anti-mouse IgG (Immunoblot grade; Bio-Rad). quent manifestation of autoimmune disease has been supported by a number of studies (1,3,7,14,20,30,31). In murine myocarditis, the consequence of inflammation or myocyte destruction or both after viral infection seems to be modulated by polyclonal anti-Id molecules (23,27,28).…”

“…The effects of monoclonal anti-Id88 in this report suggest that the anti-Id might also be acting as a CVB3 vaccine of restricted specificity. The idea of antigenic mimicry of anti-Ids has been suggested in the literature by a number of investigators (4, 8, 10, 11, 13, 18-22, 32) who studied hepatitis B infections (7,19) in addition to various other viral infections (30,33). In this connection, it is not clear whether this monoclonal anti-Id is ot (ab-2ot) or I (ab-2,B) in nature (21).…”