Comprehensive Analysis of the Tegument Proteins Involved in Capsid Transport and Virion Morphogenesis of Alpha, Beta and Gamma Herpesviruses

Viruses. 2023 Oct 6;15(10):2058. doi: 10.3390/v15102058.

Abstract

Herpesviruses are enveloped and have an amorphous protein layer surrounding the capsid, which is termed the tegument. Tegument proteins perform critical functions throughout the viral life cycle. This review provides a comprehensive and comparative analysis of the roles of specific tegument proteins in capsid transport and virion morphogenesis of selected, well-studied prototypes of each of the three subfamilies of Herpesviridae i.e., human herpesvirus-1/herpes simplex virus-1 (Alphaherpesvirinae), human herpesvirus-5/cytomegalovirus (Betaherpesvirinae) and human herpesvirus -8/Kaposi's sarcomavirus (Gammaherpesvirinae). Most of the current knowledge is based on alpha herpesviruses, in particular HSV-1. While some tegument proteins are released into the cytoplasm after virus entry, several tegument proteins remain associated with the capsid and are responsible for transport to and docking at the nucleus. After replication and capsid formation, the capsid is enveloped at the nuclear membrane, which is referred to as primary envelopment, followed by de-envelopment and release into the cytoplasm. This requires involvement of at least three tegument proteins. Subsequently, multiple interactions between tegument proteins and capsid proteins, other tegument proteins and glycoproteins are required for assembly of the virus particles and envelopment at the Golgi, with certain tegument proteins acting as the central hub for these interactions. Some redundancy in these interactions ensures appropriate morphogenesis.

Keywords: capsid transport; herpesviruses; tegument proteins; virion morphogenesis.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Capsid / metabolism
  • Capsid Proteins / metabolism
  • Herpesviridae* / metabolism
  • Herpesvirus 1, Human* / metabolism
  • Herpesvirus 8, Human* / metabolism
  • Humans
  • Morphogenesis
  • Viral Structural Proteins / metabolism
  • Virion / metabolism
  • Virus Assembly

Substances

  • Capsid Proteins
  • Viral Structural Proteins

Grants and funding

The grant 90887-2010 RGPIN from the Natural Sciences and Engineering Research Council of Canada and the grant PJT-196-150 from the Canadian Institutes of Health Research supported the research in the laboratory. VIDO receives operational funding from the Government of Saskatchewan through Innovation Saskatchewan and the Ministry of Agriculture and from the Canada Foundation for Innovation through the Major Science Initiatives.