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A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry.

Abstract：

:Herpes simplex virus type 1 (HSV-1) binds to cells through interactions of viral glycoproteins gB and gC with heparan sulfate chains on cell surface proteoglycans. This binding is not sufficient for viral entry, which requires fusion between the viral envelope and cell membrane. Here, we show that heparan sulfate modified by a subset of the multiple D-glucosaminyl 3-O-sulfotransferase isoforms provides sites for the binding of a third viral glycoprotein, gD, and for initiation of HSV-1 entry. We conclude that susceptibility of cells to HSV-1 entry depends on (1) presence of heparan sulfate chains to which virus can bind and (2) 3-O-sulfation of specific glucosamine residues in heparan sulfate to generate gD-binding sites or the expression of other previously identified gD-binding receptors.

journal_name

Cell

journal_title

Cell

authors

Shukla D,Liu J,Blaiklock P,Shworak NW,Bai X,Esko JD,Cohen GH,Eisenberg RJ,Rosenberg RD,Spear PG

doi

10.1016/s0092-8674(00)80058-6

subject

Has Abstract

pub_date

1999-10-01 00:00:00

pages

13-22

issue

1

eissn

0092-8674

issn

1097-4172

pii

S0092-8674(00)80058-6

journal_volume

99

pub_type

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