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Updated: Jul 2, 2025
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Ex Vivo Infection of Murine Epidermis with Herpes Simplex Virus Type 1
Published on: August 24, 2015
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Herpes Simplex Virus 1 Glycoprotein B from a Hyperfusogenic Virus Mediates Enhanced Cell-Cell Fusion
Katrina A Gianopulos1,2,3, Albina O Makio1,3, Suzanne M Pritchard1
1Department of Veterinary Microbiology and Pathology, College of Veterinary Medicine, Washington State University, Pullman, WA 99164, USA.
Viruses
|February 24, 2024
Summary
Herpes simplex virus 1 (HSV-1) strain ANG exhibits enhanced fusion and entry capabilities compared to wild-type strains. Specific mutations in ANG glycoproteins, particularly gB, drive this hyperfusogenic phenotype, offering insights into HSV entry mechanisms.
Area of Science:
- Virology
- Molecular Biology
- Cellular Biology
Background:
- Herpes simplex virus 1 (HSV-1) is a global pathogen responsible for considerable human illness and mortality.
- The intricate fusion and entry mechanisms of HSV-1 are not fully elucidated.
- HSV-1 strain ANG displays distinct fusion and entry characteristics compared to wild-type strains.
Purpose of the Study:
- To investigate the molecular underpinnings of the unique entry and fusion activities observed in HSV-1 strain ANG.
- To decipher the complex cascade of molecular interactions involved in HSV fusion and entry processes.
- To identify specific viral components responsible for the hyperfusogenic phenotype of HSV-1 ANG.
Main Methods:
- Comparative analysis of HSV-1 ANG and wild-type HSV-1 KOS virion fusion and entry efficiencies at different temperatures.
- Gene sequencing to identify genetic differences between HSV-1 ANG and wild-type strains, focusing on glycoproteins.
- Virus-free reporter assays to assess the fusogenic and entry capabilities of individual HSV-1 ANG glycoproteins (gB, gD, gH/gL) and their combinations.
Main Results:
- HSV-1 ANG demonstrated increased fusion with Vero cells at 4°C and enhanced entry at 15°C relative to HSV-1 KOS, indicating a hyperfusogenic phenotype.
- Genetic analysis revealed mutations in HSV-1 ANG glycoproteins gB, gC, gD, gH, and gL compared to wild-type strains.
- HSV-1 ANG gB, gD, and gH/gL were sufficient for mediating cell-cell fusion. Notably, ANG gB alone enhanced fusion when co-expressed with wild-type KOS gD and gH/gL, highlighting its hyperfusogenic potential.
Conclusions:
- The hyperfusogenic phenotype of HSV-1 strain ANG is attributed to specific mutations within its fusion and entry glycoproteins, particularly gB.
- These findings provide a valuable platform for dissecting the molecular mechanisms governing HSV fusion and cell entry.
- Understanding these mutations can lead to novel strategies for controlling HSV infections.
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