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A unique spumavirus Gag N-terminal domain with functional properties of orthoretroviral matrix and capsid

David C Goldstone1, Thomas G Flower, Neil J Ball

  • 1Division of Molecular Structure, MRC National Institute for Medical Research, the Ridgeway, Mill Hill, London, United Kingdom.

Plos Pathogens
|May 16, 2013
PubMed

Insights

Foamyviruses (FVs) share functions with other retroviruses despite distinct structures. This study reveals the structure of PFV-Gag, detailing its interaction with Env and suggesting convergent evolution of gag genes.

Area of Science:

  • Virology
  • Structural Biology
  • Molecular Evolution

Background:

  • Spumaretrovirinae (foamyviruses, FVs) infect primates, with Prototypic Foamy Virus (PFV) isolated from humans.
  • FV Gag proteins perform essential retroviral functions, yet lack sequence homology to orthoretroviral Gag.
  • Understanding FV Gag structure is crucial for explaining functional equivalence and potential zoonosis.

Purpose of the Study:

  • To investigate the structural basis for functional overlap between FV and orthoretroviral Gag proteins.
  • To elucidate the molecular mechanisms of PFV Gag-Env interaction and FV replication.
  • To examine the specificity of Trim5α restriction on PFV.

Main Methods:

  • X-ray crystallography to determine the structure of PFV Gag-NtD and its complex with the PFV Env leader peptide.
  • Biophysical and virological assays to study Gag-Env interactions and FV replication.
  • Analysis of Trim5α restriction specificity.

Main Results:

  • The crystal structure of PFV Gag-NtD reveals a unique dimeric domain unrelated to orthoretroviral Gag.
  • Detailed molecular insights into the essential Gag-Env interaction facilitating viral particle budding.
  • Data on Trim5α restriction specificity for PFV.

Conclusions:

  • Structurally distinct PFV Gag has evolved to perform functions equivalent to orthoretroviral Gag.
  • This suggests a model of convergent evolution for gag genes.
  • Provides the first structural insights into FV structural proteins and their interactions.

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