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J Biol Chem, Vol. 273, Issue 9, 5047-5052, February 27, 1998
From the 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.
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
,
,
,
, and
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
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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