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Related Experiment Videos

Characterization of Rous sarcoma virus Gag particles assembled in vitro.

F Yu1, S M Joshi, Y M Ma

  • 1Department of Molecular Biology and Genetics, Cornell University, Ithaca, New York 14853, USA.

Journal of Virology
|February 27, 2001
PubMed
Summary
This summary is machine-generated.

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Nucleic acids and specific regions of the Rous sarcoma virus (RSV) Gag protein

Area of Science:

  • Virology
  • Structural Biology
  • Biochemistry

Background:

  • Retrovirus Gag proteins self-assemble into virus-like particles (VLPs) in vitro.
  • Nucleic acid's role and the NC domain's function in Gag protein assembly are not fully understood.

Purpose of the Study:

  • To investigate the role of nucleic acids in Rous sarcoma virus (RSV) Gag protein assembly into VLPs.
  • To characterize the structural and assembly properties of RSV VLPs.
  • To identify key domains and residues within the NC domain essential for VLP assembly.

Main Methods:

  • Virus-like particle (VLP) assembly in vitro using purified RSV Gag protein and various nucleic acids.
  • Characterization of VLPs using transmission electron microscopy (TEM), scanning TEM (STEM), and cryoelectron microscopy (cryo-EM).

Related Experiment Videos

  • Site-directed mutagenesis of the NC domain to assess its role in assembly.

    • Main Results:

    • Diverse nucleic acids (RNA, ssDNA, dsDNA, heparin) efficiently promoted VLP assembly.
    • VLPs exhibited immature retroviral morphology, with a mean mass of 6.5 x 10(7) Da (approx. 1,200 Gag molecules/VLP).
    • Specific charged residues and basic residues in the NC domain, but not Zn-binding motifs, were critical for assembly.

    Conclusions:

    • Nucleic acids are essential for efficient VLP assembly from RSV Gag protein.
    • RSV VLPs serve as a valuable model for immature retroviral particles.
    • The study elucidates critical interactions within the NC domain required for Gag protein assembly.