Abstract
Herpes simplex virus type-1 (HSV-1) is one of many pathogens that use the cell surface glycosaminoglycan heparan sulfate as a receptor. Heparan sulfate is highly expressed on the surface and extracellular matrix of virtually all cell types making it an ideal receptor. Heparan sulfate interacts with HSV-1 envelope glycoproteins gB and gC during the initial attachment step during HSV-1 entry. In addition, a modified form of heparan sulfate, known as 3-O-sulfated heparan sulfate, interacts with HSV-1 gD to induce fusion between the viral envelope and host cell membrane. The 3-O-sulfation of heparan sulfate is a rare modification which occurs during the biosynthesis of heparan sulfate that is carried out by a family of enzymes known as 3-O-sulfotransferases. Due to its involvement in multiple steps of the infection process, heparan sulfate has been a prime target for the development of agents to inhibit HSV entry. Understanding how heparan sulfate functions during HSV-1 infection may not only be critical for inhibiting infection by this virus, but it may also be crucial in the fight against many other pathogens as well.
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Foundation item: NIH grant (AI 057860 to D.S)
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O’Donnell, C.D., Shukla, D. The importance of heparan sulfate in herpesvirus infection. Virol. Sin. 23, 383–393 (2008). https://doi.org/10.1007/s12250-008-2992-1
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DOI: https://doi.org/10.1007/s12250-008-2992-1
Key words
- Heparan sulfate (HS)
- Herpesviruses
- Herpes simplex virus type-1 (HSV-1)
- 3-O-sulfotransferases
- Viral entry