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Updated: Jul 19, 2026
08:26
Purification of Viral DNA for the Identification of Associated Viral and Cellular Proteins
Published on: August 31, 2017
Molecular gymnastics at the herpesvirus surface
1Unité de Virologie Structurale and Centre National de la Recherche Scientifique, Institut Pasteur, 25 Rue du Dr Roux, 75015 Paris, France. rey@pasteur.fr
EMBO Reports
|October 4, 2006
Summary
Herpes simplex virus entry involves a fusogenic signal transmitted by envelope glycoproteins. Structural insights into glycoprotein gD interactions may reveal conserved mechanisms across different virus families.
Area of Science:
- Virology
- Structural Biology
- Molecular Mechanisms
Background:
- Herpes simplex virus (HSV) entry relies on envelope glycoproteins mediating membrane fusion.
- Glycoprotein gD binding to its receptor initiates a fusogenic signal.
- This signal activates the viral fusion machinery (gB, gH, gL) for cell entry.
Purpose of the Study:
- To analyze recent structural findings on HSV envelope glycoproteins.
- To elucidate the molecular mechanism of fusogenic signal transmission.
- To compare HSV entry mechanisms with other enveloped viruses like gamma-retroviruses.
Main Methods:
- Review of recent structural biology studies.
- Analysis of glycoprotein-receptor interactions.
- Comparative analysis of viral entry mechanisms.
Main Results:
- Structural results offer clues to the molecular mechanism of fusogenic signal transmission by HSV envelope glycoproteins.
- The activation process by glycoprotein gD parallels that of gamma-retroviruses.
- Structural homology of HSV gB with rhabdovirus glycoproteins suggests functional relationships.
Conclusions:
- HSV entry mechanisms share functional similarities with simpler enveloped viruses.
- Understanding HSV glycoprotein interactions can provide insights into gamma-retrovirus entry.
- The complex entry apparatus of herpesviruses is likely functionally related to simpler enveloped viruses.
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