Detection of receptors for hepatitis B virus on cells of extrahepatic origin.

Receptors for hepatitis B virus (HBV; subtype adw) were identified on the surface of human hepatoma HepG2 cells in earlier studies. The cell receptor binding site on HBV was assigned to the preS(21-47) region of the preS1 sequence of the envelope protein. Studies presented here show that (1) amino acid residue replacements within the preS(21-47) sequence distinguishing HBV subtypes adw and ayw, preserve the binding capacity of the HBV env protein for HepG2 cell receptors; (2) the inhibition of binding between HepG2 cells and preS1-specific ligands by antibodies is effective only if the subtype specificity of anti-preS1-specific antibodies and of the preS1-specific ligands are matched; (3) receptors for HBV were present on the surface of human cells of nonhepatic origin, including peripheral blood B-lymphocytes, some hematopoietic cell lines of the B-cell lineage, neuroblastoma, amnion, and embryonic carcinoma cell lines. Receptors for HBV on these cells appeared similar to the receptor on HepG2 cells by the following criteria: (a) recognition by antibodies raised against the receptor on HepG2 cells; (b) inhibitory activity of lysates prepared from these cells on the interaction between HepG2 cells and preS1-specific ligands; and (c) the inhibitory effect of lysates from HepG2 cells on the reaction of these cells with HBsAg- and preS(21-47)-cellulose. The presence of receptors for HBV on some cells of extrahepatic origin is in accordance with earlier observations indicating that hepadnaviruses are not strictly hepatotropic.