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Related Experiment Videos

Viral DNA synthesis defects in assembly-competent Rous sarcoma virus CA mutants.

T M Cairns1, R C Craven

  • 1Department of Microbiology and Immunology, The Pennsylvania State University College of Medicine, Milton S. Hershey Medical Center, Hershey, Pennsylvania 17033, USA.

Journal of Virology
|December 19, 2000
PubMed
Summary

Mutations in the Rous sarcoma virus (RSV) major structural protein (CA) reveal the entire major homology region (MHR) is crucial for post-budding functions, impacting viral DNA synthesis and core stability.

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Area of Science:

  • Retroviral biology
  • Molecular virology
  • Protein structure-function relationships

Background:

  • The retroviral core structural protein (CA) shares a conserved major homology region (MHR) with transposable elements.
  • The function of the MHR is poorly understood due to complex mutant phenotypes in viruses and yeast TY3.
  • Previous studies have not clearly defined distinct functional subdomains within the MHR.

Purpose of the Study:

  • To investigate the functional significance of the MHR in Rous sarcoma virus (RSV) CA protein.
  • To determine if different phenotypes arise from distinct functional subdomains within the MHR.
  • To elucidate the role of the MHR in viral replication and maturation.

Main Methods:

  • Introduction of 25 specific amino acid substitutions at 10 positions within the conserved MHR of the RSV CA protein.

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  • Analysis of mutant phenotypes, including virus infectivity, assembly, budding, Gag-Pol and genome incorporation, protein processing, and endogenous viral DNA synthesis.
  • Assessment of virion core stability through detergent sensitivity assays.

    • Main Results:

    • Most substitutions were lethal, yielding one of two distinct phenotypes depending on the introduced residue.
    • Conservative substitutions often caused severe replication defects without affecting virus assembly, budding, or genome/Gag-Pol incorporation.
    • Mutant particles showed impaired endogenous viral DNA synthesis and increased core protein sensitivity to detergent, indicating MHR involvement in core formation/activity and post-budding functions.

    Conclusions:

    • The MHR appears to be essential for a critical post-budding function, as suggested by the widespread impact of mutations across the region.
    • A subset of lethal substitutions likely disrupts CA protein structure, affecting hydrophobic core or hydrogen bond networks in the carboxyl-terminal domain, impacting assembly and release.
    • The observed duality of phenotypes supports a role for the MHR in viral maturation, linking early and late stages of the retroviral life cycle.