A Novel Role for 3-O-Sulfated Heparan Sulfate in Herpes Simplex Virus 1 Entry

@article{Shukla1999ANR,
  title={A Novel Role for 3-O-Sulfated Heparan Sulfate in Herpes Simplex Virus 1 Entry},
  author={Deepak Shukla and Jian Liu and Peter Blaiklock and Nicholas W. Shworak and Xiaomei Bai and Jeffrey D. Esko and Gary H Cohen and Roselyn J Eisenberg and Robert D. Rosenberg and Patricia G. Spear},
  journal={Cell},
  year={1999},
  volume={99},
  pages={13-22}
}
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… Expand
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A role for heparan sulfate 3-O-sulfotransferase isoform 2 in herpes simplex virus type 1 entry and spread.
TLDR
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TLDR
It is demonstrated that a low-molecular-weight peptide isolated against 3-O-sulfated heparan sulfate (3-OS HS) can efficiently block HSV-2 infection and raises the possibility that 3- OS HS modifications within HS may be upregulated even more to accommodate for a significantly higher increase in the peptide binding to the infected cells. Expand
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Herpes Simplex Virus Types 1 and 2 Differ in Their Interaction with Heparan Sulfate
TLDR
B and gC homologs exhibited different patterns of sensitivity of binding to cells to inhibition with selectively N-, 2-O-, and 6-O-desulfated heparin compounds, and the O-sulfate groups of heparan sulfate were found to be more important for interaction with gB-1 than gF-2, and results indicate that HSV-1 andHSV-2 differ in their interaction with HS. Expand
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