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J Biol Chem, Vol. 273, Issue 9, 5047-5052, February 27, 1998

Interaction between Pseudorabies Virus and Heparin/Heparan Sulfate
PSEUDORABIES VIRUS MUTANTS DIFFER IN THEIR INTERACTION WITH HEPARIN/HEPARAN SULFATE WHEN ALTERED FOR SPECIFIC GLYCOPROTEIN C HEPARIN-BINDING DOMAIN

Edward Trybala, Tomas Bergström, Dorothe Spillmann^¶, Bo Svennerholm, Shannon J. Flynn, and Patrick Ryan

From the  Department of Clinical Virology, University of Göteborg, Guldhedsgatan 10B, S-413 46 Göteborg, Sweden, the ^¶ Department of Medical and Physiological Chemistry, University of Uppsala, S-751 23 Uppsala, Sweden, and the  Department of Microbiology and Immunology, University of Tennessee, Memphis, Tennessee 38163

Cell surface heparan sulfate serves as an initial receptor for a number of herpesviruses including pseudorabies virus (PrV). It has been demonstrated that the heparan sulfate-binding domain of PrV glycoprotein C is composed of three discrete clusters of basic residues corresponding to amino acids 76-RRKPPR-81, 96-HGRKR-100, and 133-RFYRRGRFR-141, respectively, and that these clusters are functionally redundant, i.e. each of them could independently support PrV attachment to cells (Flynn, S. J., and Ryan, P. (1996) J. Virol. 70, 1355-1364). To evaluate the functional significance of each of these clusters we have used PrV mutants in which, owing to specific alterations in glycoprotein C, the heparan sulfate-binding site is dominated by a single specific cluster. These mutants exhibited different patterns of susceptibility to selectively N-, 2-O-, and 6-O-desulfated heparin preparations in virus attachment/infectivity assay. Moreover PrV mutants differed as regard to efficiency of their attachment to and infection of cells pretreated with relatively low amounts of heparan sulfate-degrading enzymes. Furthermore glycoprotein C species, purified from respective mutants, bound heparin oligosaccharide fragments of different minimum size. These differences suggest that specific clusters of basic amino acids of the heparan sulfate-binding domain of glycoprotein C may support PrV binding to different structural features/stretches within the heparan sulfate chain.

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