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Cryo-EM structure of the Rous sarcoma virus octameric cleaved synaptic complex intasome.

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Rous sarcoma virus integrase (IN) forms diverse intasome structures. This study reveals key assembly steps and conformational changes, showing flexibility in IN dimers is crucial for capturing target DNA during retroviral integration.

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Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • Retroviral intasomes, complexes of integrase (IN) and viral DNA, exhibit structural diversity despite conserved integration mechanisms.
  • Understanding intasome assembly is crucial for deciphering retroviral replication strategies.

Purpose of the Study:

  • To investigate the assembly mechanisms of Rous sarcoma virus (RSV) intasomes.
  • To determine the structure of the RSV octameric intasome and identify key conformational changes during assembly.

Main Methods:

  • Single particle cryo-electron microscopy was used to determine the structure of the RSV octameric intasome.
  • In vitro assays and infectivity studies were performed using site-directed mutagenesis of IN C-terminal domain.

Main Results:

  • The structure of the RSV octameric intasome revealed flexibility in distal IN dimers and movement within the intasome core, suggesting ordered conformational transitions.
  • Amino acid substitutions in the IN C-terminal domain impacted intasome assembly, function, and viral infectivity.
  • Unexpectedly, the 17 C-terminal amino acids of IN were dispensable for infection, though they regulated tetrameric to octameric intasome transitions in vitro.

Conclusions:

  • RSV intasome assembly involves ordered conformational transitions, with flexible distal IN dimers potentially playing a role in target DNA capture.
  • The C-terminal domain of RSV IN has a complex role in intasome maturation and viral infectivity, with a dispensable region for infection identified.