Characterisation of the polymerised and monomeric human serum albumin binding sites on hepatitis B surface antigen.

Receptors for polymerised human albumin are present on the pre-S sequence of the envelope protein of HBV and on the hepatocyte membrane and are thought to be involved in uptake of the virus by hepatocytes. Using a solid phase radioimmunoassay we demonstrate binding of HBsAg to polymerised human serum albumin (pHSA) in both HBe antigen-positive and -negative patients, and this binding is linearly related to the HBsAg titre in both groups. There are probably several modes of interaction between HBsAg and pHSA. Here we show that pHSA binds to the 22,000-dalton polypeptide of HBsAg, which does not contain the pre-S sequence. This pHSA-HBsAg interaction is inhibited by physiological concentrations of human serum albumin, suggesting that the albumin known to be present in the envelop of HBsAg plays a role in this binding. The inhibition of pHSA/HBsAg interaction by native albumin suggests that this interaction is probably not an important mechanism of virus uptake during infection of hepatocytes.