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Related Experiment Video

Updated: Sep 2, 2025

Temporal Analysis of the Nuclear-to-cytoplasmic Translocation of a Herpes Simplex Virus 1 Protein by Immunofluorescent Confocal Microscopy
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Conformational Changes in Herpes Simplex Virus Glycoprotein C.

Katrina A Gianopulos1,2,3, Tri Komala Sari1,3,4, Darin J Weed1,3

  • 1Department of Veterinary Microbiology and Pathology, College of Veterinary Medicine, Washington State Universitygrid.30064.31, Pullman, Washington, USA.

Journal of Virology
|August 1, 2022
PubMed
Summary
This summary is machine-generated.

Herpes simplex virus 1 (HSV-1) uses a low-pH pathway for cell entry, regulated by glycoprotein C (gC). This study shows gC undergoes pH-induced changes, crucial for HSV-1 entry.

Keywords:
conformational changeendocytosisendosomal pHgCglycoproteinsherpes simplex virusherpesvirusesmembrane fusionviral entry

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Area of Science:

  • Virology
  • Cell Biology
  • Molecular Biology

Background:

  • Herpes simplex virus 1 (HSV-1) is a significant human pathogen with multiple entry mechanisms.
  • HSV-1 entry involves low-pH and neutral-pH pathways, with glycoprotein B (gB) mediating fusion.
  • Glycoprotein C (gC) is known to mediate HSV-1 attachment but its role in entry is complex.

Purpose of the Study:

  • To investigate the role of HSV-1 glycoprotein C (gC) in low-pH-mediated viral entry.
  • To determine if gC undergoes conformational changes in response to low pH.
  • To elucidate the importance of gC's N-terminal region in the low-pH entry pathway.

Main Methods:

  • Treatment of HSV-1 virions with low pH and analysis of conformational changes in gC using antibody binding assays.
  • Characterization of gC epitopes sensitive to pH changes.
  • Inhibition of HSV-1 entry using a monoclonal antibody targeting a specific gC epitope.

Main Results:

  • Mildly acidic pH triggers conformational changes in HSV-1 gC, indicated by altered antigenic epitopes.
  • These pH-induced conformational changes in gC are reversible.
  • A monoclonal antibody targeting an N-terminal gC epitope, which undergoes pH-induced changes, inhibited low-pH HSV-1 entry.

Conclusions:

  • HSV-1 gC plays a critical role in facilitating viral entry via the low-pH endocytosis pathway.
  • gC positively regulates pH-triggered conformational changes in the fusion protein gB.
  • The N-terminal region of gC is important for its function in the low-pH entry route, offering new insights into herpesvirus entry mechanisms.