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Updated: Aug 17, 2026

Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling
Published on: February 5, 2018
Glycoprotein B (gB) of pseudorabies virus interacts specifically with the glycosaminoglycan heparin
D Sawitzky1, A Voigt, H Zeichhardt
1Institute for Clinical and Experimental Virology, Free University Berlin, Germany. dirks@zedat.fu-berlin.de
Abstract:
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.
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