The Vero cell receptor for the hepatitis B virus small S protein is a sialoglycoprotein.

The Vero (African green monkey kidney-derived) cell line is capable of binding recombinant hepatitis B surface antigen (rHBsAg) particles containing only the small surface (S) protein of hepatitis B virus (HBV). This binding activity appears to be due to a single major population of receptors (M. E. Peeples et al., Virology 160, 135-142 (1987]. Since infectious HBV particles also contain the small S protein, it is possible that the Vero cell receptor might also function as an HBV receptor. The initial physical characterization of this receptor is reported here. Treatment of Vero cells with each of four proteases reduced their binding activity by 70% or greater, indicating that the receptor is partially protein in nature. Binding activity was also reduced by pretreating cells with neuraminidase or low levels of sodium periodate, indicating that sialic acid also plays a major role in the receptor activity. Consistent with this interpretation, N-acetylneuraminic acid and N-acetylneuraminyl-lactose were able to competitively inhibit rHBsAg particle attachment to Vero cells. The protein nature of the Vero cell receptor was confirmed by the demonstration that chymotrypsin treatment which resulted in 70% loss of binding had little effect on the cell sialic acid content. Therefore, the Vero cell receptor for rHBsAg particles is a sialoglycoprotein.