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Updated: Mar 26, 2026

Temporal Analysis of the Nuclear-to-cytoplasmic Translocation of a Herpes Simplex Virus 1 Protein by Immunofluorescent Confocal Microscopy
Published on: November 4, 2018
gH/gL supercomplexes at early stages of herpesvirus entry
1Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111, USA.
Insights
Herpesvirus entry involves complex glycoprotein interactions. Understanding these molecular mechanisms, particularly the signal relay to the fusogen gB, is crucial for future antiviral strategies.
Area of Science:
- Virology
- Structural Biology
- Molecular Biology
Background:
- Herpesvirus entry into host cells relies on intricate glycoprotein interactions.
- Key proteins include the receptor-binding protein, heterodimer gH/gL, and fusogen gB.
- While individual structures exist, high-order glycoprotein complexes remain poorly understood.
Purpose of the Study:
- To elucidate the structural mechanisms of herpesvirus entry.
- To understand how signals are transmitted from receptor-binding proteins to the fusogen gB.
- To investigate the role of gH/gL in membrane fusion.
Main Methods:
- Analysis of recent crystal structures of glycoprotein complexes.
- Investigating dynamic intermediate complexes.
- Focus on human cytomegalovirus and Epstein-Barr virus systems.
Main Results:
- Structures of early-stage entry complexes reveal mechanisms controlling viral tropism.
- Dynamic intermediate complexes involving gH/gL were identified.
- These complexes may directly mediate membrane deformation and juxtaposition.
Conclusions:
- Recent structural insights advance understanding of herpesvirus entry.
- The signal relay pathway to the fusogen gB is a critical area for future research.
- Further structural studies are needed to fully map the fusion mechanism.
Abstract:
Membrane fusion during herpesvirus entry into host cells is a complex process where multiple glycoproteins interact to relay the triggering signal from a receptor-binding protein to the conserved fusogen gB through the conserved heterodimer gH/gL. Crystal structures of individual glycoproteins are available, yet high-order 'supercomplexes' have been elusive. Recent structures of complexes between gH/gL from human cytomegalovirus or Epstein-Barr virus and the receptor-binding proteins that form at early stages of herpesviral entry highlighted mechanisms that control tropism and revealed dynamic intermediate complexes containing gH/gL that may directly participate in membrane deformation and juxtaposition. Determining how the triggering signal reaches the fusogen gB represents the next frontier in structural biology of herpesvirus entry.
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