The present study confirms our previous findings made by using heparin affinity chromatography that bovine herpesvirus 1 gB can bind to heparin-like structures. In order to locate the functional domain for heparin binding, we expressed the extracellular portion of gB (gBt) and the large subunit of gB (gBb) in Madin Darby bovine kidney (MDBK) cells under the control of the bovine heat shock protein 70A gene promoter. The recombinant gBt and gBb were both efficiently secreted from the transfected cells. They were shown to have structural and antigenic properties similar to those of authentic gB. Like authentic gB, both gBt and gBb were able to bind heparin-Sepharose as well as heparan sulfates on MDBK cells. Thus, we suggest that at least one heparin-binding domain is localized in gBb, the N-terminal portion of gB, which agrees with the presence of clusters of prolines and basic residues, thought to be essential for heparin binding
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