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Capsid flexibility during Ty1 virus-like particle assembly.

Bryan S Sibert1,2,3, J Adam Hannon-Hatfield4, Giuseppe Nicastro5

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The Ty1 retrotransposon forms virus-like particles (VLPs) with diverse structures, not true icosahedral shapes. This heterogeneity arises from flexible Gag protein assembly, revealing new insights into LTR retrotransposon organization.

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Area of Science:

  • Structural biology
  • Molecular biology
  • Virology

Background:

  • The Ty1/Copia family (Pseudoviridae) comprises LTR retrotransposons found in eukaryotes, sharing ancestry with retroviruses.
  • Ty1 retrotransposons assemble into virus-like particles (VLPs) primarily composed of Gag and Gag-Pol proteins.

Purpose of the Study:

  • To determine the structural organization and Gag protein interactions within Ty1 VLPs.
  • To elucidate the mechanisms underlying the heterogeneous morphology of Ty1 VLPs.

Main Methods:

  • Cryo-electron tomography (cryo-ET) of purified Ty1 VLPs.
  • Sub-tomogram averaging (STA) to generate high-resolution EM density maps.
  • X-ray crystallography and solution NMR for modeling protein domains (CA-CTD and CA-NTD).

Main Results:

  • Identified unique pentagonal and hexagonal capsomere structures within Ty1 VLPs.
  • Demonstrated that Ty1 VLPs exhibit diverse capsomere arrangements, unlike icosahedral virions.
  • Modeled the Ty1 Gag capsid C-terminal domain (CA-CTD) and N-terminal domain (CA-NTD), revealing flexibility at Interface-2 crucial for assembly.
  • Linked capsomere flexibility to the heterogeneous VLP size and morphology.

Conclusions:

  • Ty1 VLPs possess a non-icosahedral, heterogeneous structure due to flexible Gag protein assembly.
  • The structural plasticity of Ty1 Gag proteins allows for diverse capsomere arrangements, explaining VLP heterogeneity.
  • Findings provide a deeper understanding of LTR retrotransposon assembly and evolution.