Glycoprotein B (gB) of pseudorabies virus interacts specifically with the glycosaminoglycan heparin.
We have previously shown that the pseudorabies virus (PrV) glycoproteins gB and gC (former PrV-gII and PrV-gIII) exhibit heparin-binding properties. While PrV-gC functions as the major adsorption protein, the biological role of the heparin-binding properties of PrV-gB are not understood. We used a gC-deleted PrV-mutant, PrV (dlg92/dltk), to analyse the heparin-binding properties of PrV-gB and the biological role of the PrV-gB-protein in adsorption. PrV-gB was the only glycoprotein of this vaccine strain binding to immobilised heparin in in vitro assays. Presence of the gC-protein was not necessary for the interaction of gB with heparin. Soluble heparin also interfered with adsorption of this mutant virus to a similar extent as it blocked adsorption of wild-type PrV (Ka), but it had only a minor inhibitory effect on infectivity of the mutant strain. These results show that PrV-gB interacts specifically with immobilized heparin and heparin-like structures on the cell surface, but this interaction is not required for a productive infection.
Sawitzky
D
D
Institute for Clinical and Experimental Virology, Free University Berlin, Germany. dirks@zedat.fu-berlin.de
Voigt
A
A
Zeichhardt
H
H
Habermehl
K O
KO
D000327:Adsorption; D002460:Cell Line; D006025:Glycosaminoglycans / Q000378:metabolism*; D006493:Heparin / Q000378:metabolism*; D011558:Herpesvirus 1, Suid / Q000378:metabolism* / Q000472:pathogenicity; D011485:Protein Binding; D012995:Solubility; D014759:Viral Envelope Proteins / Q000378:metabolism*
D006025:Glycosaminoglycans; D014759:Viral Envelope Proteins; C070915:glycoprotein gII, pseudorabies virus; C042966:pseudorabies virus glycoproteins; D006493:Heparin