Secretion of polyalbumin receptors in vitro

The nature of hepatitis B surface antigen (HBsAg)-associated receptors for polymerized human serum albumin (pHSA-R) and their relationship to hepatitis B e antigen (HBeAg) and human serum proteins have not been defined. We studied by radioimmunoassay and by electron microscopy HBsAg-associated pHSA-R secreted in vitro by a human hepatocellular carcinoma cell line (PLC/PRF/5) and by mouse 3T3 fibroblasts after transfection with cloned hepatitis B virus (HBV) DNA (4.10 cells). PLC/PRF/5 cells expressed only HBsAg, whereas 4.10 cells secreted also HBeAg. There was no significant difference in the production of HBsAg, HBeAg, and pHSA-R when the cells were cultured in the presence or absence of fetal calf serum. Secretion of pHSA-R by the two cell lines for a given amount of HBsAg was equal irrespective of the presence or absence of HBeAg. Supernatants from both cell lines grown in serum-free medium did not contain any Clq or albumin when tested by immunodiffusion. The ability of a transfected mouse cell line to produce HBsAg with pHSA-R activity strongly suggests that pHSA-R is coded by the HBV genome and does not depend on the presence of human serum proteins. In addition, our findings fail to demonstrate any correlation between HBeAg production and pHSA-R.