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[Paramyxovirus budding]

Takashi Irie1, Takemasa Sakaguchi

  • 1Department of Virology, Graduate School of Biomedical Sciences, Hiroshima University, Hiroshima 734-8551, Japan. tirie@hiroshima-u.ac.jp

Uirusu
|November 28, 2007
PubMed

Insights

Enveloped viruses utilize L-domain motifs to interact with host cell machinery for budding. This review explores paramyxovirus budding, focusing on the role of the endosomal sorting complex required for transport (ESCRT) pathway.

Area of Science:

  • Virology and Molecular Biology
  • Cellular Biology
  • Biochemistry

Context:

  • Enveloped virus budding is a critical process for viral replication and spread.
  • L-domain motifs in viral proteins mediate interactions with host cellular machinery.
  • The endosomal sorting complex required for transport (ESCRT) pathway is known to be involved in the budding of many enveloped viruses.

Purpose:

  • To review the current understanding of enveloped virus budding mechanisms.
  • To specifically investigate the budding process of paramyxoviruses.
  • To discuss the potential involvement of host cellular MVB sorting machinery in paramyxovirus budding, particularly concerning L-domain motifs and ESCRT pathway dependency.

Summary:

  • Viral L-domain motifs facilitate virus budding by interacting with host proteins involved in endocytosis and multi-vesicular body (MVB) sorting.
  • The cellular Vps4 enzyme, crucial for ESCRT machinery disassembly, is often implicated in the final stages of enveloped virus budding.
  • This review focuses on paramyxoviruses, examining their budding mechanisms where L-domain motifs are not yet identified and MVB involvement is unclear.

Impact:

  • Highlights knowledge gaps in enveloped virus budding, particularly for viruses lacking identified L-domains.
  • Provides insights into the specific budding strategies of paramyxoviruses.
  • Contributes to a deeper understanding of host-pathogen interactions during viral replication, potentially informing antiviral strategies.

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