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

First Author  Shukla D Year  1999
Journal  Cell Volume  99
Issue  1 Pages  13-22
PubMed ID  10520990 Mgi Jnum  J:62990
Mgi Id  MGI:1860201 Doi  10.1016/s0092-8674(00)80058-6
Citation  Shukla D, et al. (1999) A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry. Cell 99(1):13-22
abstractText  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.
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