Mapping of heparin-binding structures on bovine herpesvirus 1 and pseudorabies virus gIII glycoproteins
- PMID: 7683156
- DOI: 10.1006/viro.1993.1254
Mapping of heparin-binding structures on bovine herpesvirus 1 and pseudorabies virus gIII glycoproteins
Abstract
The gIII glycoproteins of both bovine herpesvirus 1 (BHV 1) and pseudorabies virus (PrV) mediate the initial and dominant interactions between virus and permissive host cells. By studying virus binding to wild-type and heparin-deficient CHO cells, we demonstrated that the cellular heparin-like moieties play an essential role in BHV 1 and PrV gIII-mediated virus attachment. Subsequent studies were carried out to map the gIII structures that are responsible for heparin binding. First, based on the observation that BHV 1 and PrV are differentially sensitive to heparin inhibition of gIII-mediated attachment to cells, we conducted a gIII domain shuffling experiment. This involved the construction of a set of recombinant BHV 1 expressing BHV 1 and PrV gIII chimeras and then using the sensitivity to heparin inhibition as a means of mapping the potential heparin-binding regions on the gIII molecules. Next, we synthesized panels of partially overlapping BHV 1 and PrV gIII peptides and examined their reactivity to heparin. The results from these experiments demonstrated five heparin-binding sites between amino acid 129 and 310 of BHV 1 gIII and four heparin-binding sites between amino acid 90 and 275 of PrV gIII.
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