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Ex Vivo Infection of Murine Epidermis with Herpes Simplex Virus Type 1
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Entry of Alphaherpesviruses.

Tina M Cairns1, Sarah A Connolly2

  • 1Department of Microbiology, School of Dental Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA.

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|August 9, 2020
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Summary
This summary is machine-generated.

Alphaherpesviruses use essential glycoproteins like glycoprotein D (gD) to enter cells. Structural studies reveal how these proteins interact and change shape during viral entry, though coordination mechanisms require further investigation.

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Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • Alphaherpesviruses are enveloped viruses that infect cells via membrane fusion.
  • Viral entry relies on essential glycoproteins: glycoprotein D (gD), gHgL, and gB.
  • gD is unique to alphaherpesviruses and acts as the receptor-binding protein.

Purpose of the Study:

  • To elucidate the structural basis of alphaherpesvirus entry.
  • To understand the roles and interactions of key viral glycoproteins (gD, gHgL, gB).
  • To investigate conformational changes during the viral fusion process.

Main Methods:

  • Structural studies of viral glycoproteins using X-ray crystallography and cryo-electron tomography.
  • Functional studies involving receptor binding, antibody mapping, and interspecies chimeric constructs.
  • Comparative structural analysis of different glycoprotein conformations.

Main Results:

  • Structural insights into receptor-bound and unliganded gD reveal conformational changes upon binding.
  • Mapping of neutralizing antibodies and chimeric gHgL constructs identified interaction sites for gD and gB.
  • Cryo-electron tomography revealed substantial refolding of gB during membrane fusion.

Conclusions:

  • Structural and functional studies provide significant insights into the alphaherpesvirus entry mechanism.
  • Conformational changes in gD and gB are critical for viral entry.
  • Further research is needed to fully understand the coordinated interactions of these glycoproteins during entry.