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Importance of Viral Late Domains in Budding and Release of Enveloped RNA Viruses

Lisa Welker1, Jean-Christophe Paillart1, Serena Bernacchi1

  • 1Architecture et Réactivité de l'ARN, UPR 9002, IBMC, CNRS, Université de Strasbourg, F-67000 Strasbourg, France.

Viruses
|August 28, 2021
PubMed

Insights

Late assembly (L) domains are crucial for viral replication, mediating virion release by engaging cellular ESCRT machinery. This review focuses on L domain types and their roles in RNA virus budding, particularly in retroviruses.

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Late assembly (L) domains are conserved protein sequences essential for the final stages of viral replication.
  • These domains function as adaptors, recruiting cellular ESCRT machinery to facilitate membrane fission and virion release.
  • Mutations in L domains lead to the accumulation of immature virions at the plasma membrane.

Purpose of the Study:

  • To review the current understanding of different L domain classes and their mechanisms.
  • To highlight the cellular partners involved in viral budding mediated by L domains.
  • To focus on the role of L domains in the replication of retroviruses and other enveloped RNA viruses.

Main Methods:

  • Literature review and synthesis of existing research on viral L domains.
  • Analysis of conserved sequence motifs and their functional implications.
  • Examination of studies investigating L domain interactions with the ESCRT pathway.

Main Results:

  • Identified three main classes of L domains: PT/SAP, YPXnL/LXXLF, and PPxY.
  • Discussed the involvement of L domains in various enveloped RNA viruses, including retroviruses, arenaviruses, filoviruses, rhabdoviruses, reoviruses, and paramyxoviruses.
  • Highlighted emerging evidence for additional L domain motifs.

Conclusions:

  • L domains are critical viral determinants for efficient virion release through interaction with host ESCRT factors.
  • Understanding L domains provides insights into viral pathogenesis and potential therapeutic targets.
  • Further research is needed to fully elucidate the diversity and mechanisms of L domains in viral budding.
Keywords:
ESCRT machineryRNA enveloped virusesbuddinglate assembly domainsretroviral gag precursorretrovirusstructural viral proteinsubiquitinationviral assembly

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