Related Experiment Video
Updated: Jun 13, 2026

Purification of Viral DNA for the Identification of Associated Viral and Cellular Proteins
Published on: August 31, 2017
The virion host shutoff endonuclease (UL41) of herpes simplex virus interacts with the cellular cap-binding complex
Heidi G Page1, G Sullivan Read
1Division of Cell Biology and Biophysics, School of Biological Sciences, University of Missouri-Kansas City, 5007 Rockhill Road, Kansas City, MO 64110, USA.
Abstract:
The herpes simplex virus Vhs endonuclease degrades host and viral mRNAs. Isolated Vhs cuts any RNA at many sites. Yet, within cells, it targets mRNAs and cuts at preferred sites, including regions of translation initiation. Previous studies have shown that Vhs binds the translation factors eIF4A and eIF4H. Here, we show that Vhs binds the cap-binding complex eIF4F. Association with eIF4F correlated with the ability of Vhs to bind eIF4A but not eIF4H. All Vhs proteins that degrade mRNAs associated with eIF4F. However, simply tethering an active endonuclease to eIF4F is not sufficient to degrade mRNAs. Binding to eIF4H may also be required.
More Related Videos
Related Concept Videos
Inhibitors Of Virion Release
Antiviral Nucleoside Inhibitors
Inhibitors of Virion Maturation and Assembly
Retrovirus Life Cycles
Retroviruses
Immune Response Against Viral Pathogens
NK Cells
NK cells are a crucial part of our innate immune system, acting as the first line of defense against viral infections. These cells can recognize and kill infected cells without prior exposure to the virus, effectively slowing down the spread of infection. Additionally, NK cells produce proinflammatory...

