[Paramyxovirus budding]

Uirusu. 2007 Jun;57(1):1-7. doi: 10.2222/jsv.57.1.
[Article in Japanese]

Abstract

Our knowledge about envelope virus budding has been dramatically increased, since L-domain motifs were identified within their matrix and retroviral Gag proteins which drive virus budding. These viral proteins have been shown to interact with host cellular proteins involved in endocytosis and/or multi-vesicular body (MVB) sorting via their L-domains. Since budding of many enveloped viruses have been reported to be dependent on the activity of cellular Vps4, which catalyzes the disassembly of ESCRT machinery in the final step of protein sorting, this cellular function is believed to be utilized for efficient virus budding. However, for many enveloped viruses, L-domain motifs have not yet been identified, and the involvement of MVB sorting machinery in virus budding is still unknown. In this review, we will focus on paramyxoviruses among such viruses, and discuss their budding with the latest information.

Publication types

  • English Abstract
  • Review

MeSH terms

  • Animals
  • Cell Membrane / virology
  • Cytoplasm / virology
  • Endocytosis
  • Humans
  • Paramyxoviridae / growth & development
  • Paramyxoviridae / physiology*
  • Protein Structure, Tertiary
  • Protein Transport
  • Viral Proteins / chemistry
  • Viral Proteins / physiology
  • Virus Assembly
  • Virus Replication

Substances

  • Viral Proteins