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Identification of the glycosaminoglycan-binding site on the glycoprotein E^rns of bovine viral diarrhoea virus by site-directed mutagenesis

Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury RG20 7NN, UK¹

Author for correspondence: Munir Iqbal. Fax +44 1635 577263. e-mail munir.iqbal{at}bbsrc.ac.uk

Bovine viral diarrhoea virus (BVDV) envelope glycoprotein E^rns interacts with highly sulphated heparin-like glycosaminoglycans (GAGs) located on the cell surface as an early step in virus infection of cells. Site-directed mutagenesis of recombinant E^rns was undertaken and analysis of mutants by heparin-affinity chromatography and cell surface binding showed that a cluster of basic amino acids (⁴⁸⁰KKLENKSK⁴⁸⁷) near the C terminus of E^rns was essential for binding. Mutants with amino acid substitutions of lysine residues 481 and 485 in E^rns reduced the binding of E^rns to immobilized heparin and cellular GAGs but retained ribonuclease activity. In contrast to normal E^rns, E^rns that was unable to bind to cells also failed to inhibit BVDV infection of cells when the cells were pre-incubated with E^rns. It is proposed that the cluster of basic residues (⁴⁸⁰KKLENKSK⁴⁸⁷) localized at the C-terminal end of E^rns constitutes a GAG-binding site.

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