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Early Viral Entry Assays for the Identification and Evaluation of Antiviral Compounds
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Entry of betaherpesviruses.

Mitsuhiro Nishimura1, Yasuko Mori1

  • 1Division of Clinical Virology, Center for Infectious Diseases, Kobe University Graduate School of Medicine, Kobe, Japan.

Advances in Virus Research
|August 24, 2019
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Summary

Betaherpesvirus entry mechanisms, including human cytomegalovirus (HCMV) and human herpesvirus 6A/6B (HHV-6A/6B), involve complex viral glycoprotein interactions with specific host cell receptors, dictating distinct cellular tropisms and pathogenesis.

Keywords:
BetaherpesvirusEntryHuman cytomegalovirusHuman herpesvirus 6AHuman herpesvirus 6B

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Area of Science:

  • Virology
  • Molecular Biology
  • Immunology

Background:

  • Betaherpesviruses, including human cytomegalovirus (HCMV) and human herpesviruses 6A and 6B (HHV-6A/6B), are significant human pathogens.
  • HCMV utilizes distinct viral glycoprotein complexes (trimer and pentamer) for entry into diverse cell types, mediated by the fusion protein gB.
  • HHV-6A and HHV-6B, despite high genomic similarity, exhibit different epidemiological and clinical roles, with HHV-6B causing exanthema subitum and potential encephalitis post-transplant.

Purpose of the Study:

  • To provide an overview of betaherpesvirus entry mechanisms.
  • To highlight recent advances in understanding HCMV and HHV-6 entry pathways.
  • To elucidate the roles of specific viral glycoproteins and host cell receptors in viral tropism and pathogenesis.

Main Methods:

  • Review of current literature on betaherpesvirus entry.
  • Analysis of structural and functional data for viral glycoproteins.
  • Identification and characterization of viral entry receptors.

Main Results:

  • HCMV employs the gH/gL/gO trimer for fibroblast entry and the gH/gL/UL128/UL130/UL131 pentamer for epithelial/endothelial cell entry, binding to PDGFRα and Nrp2, respectively.
  • Atomic structures of HCMV fusion protein gB and the pentamer have been determined, alongside in situ visualization of virion glycoproteins.
  • HHV-6A and HHV-6B utilize distinct entry receptors: CD46 for HHV-6A and CD134 for HHV-6B, mediated by their respective gH/gL/gQ1/gQ2 complexes.

Conclusions:

  • Viral entry mechanisms for betaherpesviruses are intricate, involving specific glycoprotein-receptor interactions.
  • Distinct receptor usage by HHV-6A and HHV-6B explains their differing pathogenesis and cellular tropisms.
  • Further research into these entry pathways can inform therapeutic strategies against these important viruses.