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(Received for publication, July 1, 1997)
,
and
From the Cell surface heparan sulfates mediate primary
attachment of herpes simplex virus type 1, the first step in virus
invasion of the cells. Removal of the host cell heparan sulfate results in a significantly diminished susceptibility of the cell to virus infection. On the virus envelope, glycoprotein C has been identified as
the major binding site for heparan sulfate in the primary attachment of
the virus to host cells. Using selectively desulfated heparins and metabolically labeled host cell heparan sulfate, we have
analyzed the structural requirements of heparan sulfate to provide
binding sites for glycoprotein C and the whole virus. Employing
glycoprotein C affinity chromatography and a virus binding assay, we
subfractionated oligosaccharides derived from heparan sulfate and
partially desulfated heparin into selectively bound and unbound pools.
These were chemically depolymerized and analyzed at the disaccharide
level. The shortest glycoprotein C-binding fragment consisted of 10-12
monosaccharide units containing at least one 2-O- and one
6-O-sulfate group that have to be localized in a
sequence-specific way, based on the finding that bound and unbound HS
fragments do not differ in charge or composition. The binding sequence
is found within N-sulfated blocks of heparan sulfate,
although several N-acetyl groups can be tolerated within
the minimal binding sequence. These minimal requirements for herpes
simplex virus type 1 binding to heparan sulfate are clearly distinct
from other identified protein binding sites.
Department of Medical and Physiological
Chemistry,
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