The interaction of the glycoprotein gB of Aujesky's disease virus (ADV, Suid herpesvirus 1) with heparan sulfates of BHK-21 cells was studied. The study used the native glycoprotein gB purified from the virus envelope by affinity chromatography based on gB-specific monoclonal antibodies. The cellular binding of the glycoprotein gB was specific and dose-dependent. Heparin, a structural analogue of heparan sulfates, inhibited the cellular binding of gB. The herapinase treatment of cells also resulted in the inhibition of the cellular binding of gB. The purified glycoprotein gB bound to heparin-Sepharose and was specifically eluated by heparin. The denaturation of gB was followed by 70-80% decreases in its binding to Sepharose-immobilized heparin. The findings may lead to the conclusion that plasma cell membranous heparan sulfates are one of the glycoprotein gB receptors in ADV. At the same time the heparin-binding site of ADV gB is at least partially conformation-dependent.