Characterization of the interaction between polymerized human albumin and hepatitis B surface antigen.
The interaction of polymerized human albumin with hepatitis B surface antigen was characterized utilizing a solid-phase radioimmunoassay. The interaction was specific as shown by quantitative inhibition of binding by soluble polymerized human albumin. The interaction was species restricted in that hepatitis B surface antigen did not bind nonhuman polymerized albumins. The albumin polymer size was critical to the binding reaction as was the concentration of hepatitis B surface antigen; the interaction was also temperature, ionic strength, and pH dependent. Hepatitis B e antigen positive sera possessed greater polyalbumin binding reactivity than hepatitis B e antigen negative sera. This interaction was shown to be inhibited by normal human serum which suggested that the polyalbumin receptor on hepatitis B surface antigen may be a host rather than viral component. In view of our previous observation that polymerized human albumin binds human C1q, the interactions between polymerized human albumin, hepatitis B surface antigen, and human C1q may be relevant to hepatitis B virus-host receptor mechanisms.
D000818:Animals; D001666:Binding Sites, Antibody; D002850:Chromatography, Gel; D000939:Epitopes; D006514:Hepatitis B Surface Antigens / Q000032:analysis*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007106:Immune Sera; D011817:Rabbits; D011863:Radioimmunoassay; D012709:Serum Albumin / Q000032:analysis*; D013696:Temperature
D000939:Epitopes; D006514:Hepatitis B Surface Antigens; D007106:Immune Sera; D012709:Serum Albumin