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Daniel Matthes1, Tatiana Wiktorowicz, Juliane Zahn

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Foamy virus (FV) Gag proteins primarily use arginine over lysine, a feature crucial for replication in primary cells. Replacing arginine with lysine impairs viral replication, especially under interferon treatment, suggesting lysines may prevent proteasomal degradation.

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Area of Science:

  • Virology
  • Molecular Biology
  • Protein Biochemistry

Background:

  • Foamy viruses (FV) exhibit a unique characteristic of having predominantly arginine residues instead of lysines in their Gag proteins, suggesting evolutionary selection.
  • The functional significance of this arginine-rich motif in FV Gag proteins remains largely unexplored.

Purpose of the Study:

  • To investigate the functional role of lysine residues in the Gag protein of prototypic foamy virus (PFV) during its replication cycle.
  • To determine if introducing lysines at arginine-specific positions impacts viral replication, particle formation, and host immune responses.

Main Methods:

  • Construction and analysis of infectious molecular clones of PFV with specific lysine substitutions in the Gag protein.
  • Assessment of viral replication in permanent and primary cell cultures.
  • Evaluation of viral particle formation, including virus-like particles (VLPs) and pseudotyping.
  • Analysis of viral restriction factors, such as tetherin (CD317) and Trim5α, and response to interferon (IFN) treatment.

Main Results:

  • Most Gag lysine mutants replicated similarly to wild-type (wt) PFV in permanent cell lines and showed genetic stability.
  • Mutants exhibited normal late reverse transcription, virion DNA content, and infectiousness.
  • Several lysine mutants were ubiquitinated but failed to form VLPs or undergo pseudotyping.
  • A significant replicative disadvantage was observed for most mutants in primary cells, exacerbated by IFN treatment.
  • No increased restriction by tetherin or Trim5α was detected for lysine mutants.
  • A single lysine substitution, non-essential in permanent cells, severely impaired replication in primary cells, even without IFN.

Conclusions:

  • The paucity of lysines in FV Gag proteins is critical for efficient replication in primary cells, potentially linked to preventing proteasomal degradation.
  • Specific lysine residues in PFV Gag play essential roles in viral replication, particularly in non-permissive cellular environments or under immune pressure.
  • The observed phenotypes suggest a complex interplay between Gag protein lysine content, viral replication, and host innate immunity.