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Structural organization of murine intracisternal A particles.
Journal of Virology
|February 1, 1973
Summary
Murine intracisternal A particles possess unique structures, differing from oncogenic RNA tumor viruses. Their inner shell, containing a major protein, is stabilized by disulfide bonds, resisting detergent and SDS treatments.
Area of Science:
- Virology
- Structural Biology
- Biochemistry
Background:
- Murine intracisternal A particles (A particles) are retroviral elements with distinct structural characteristics.
- Understanding A particle structure is crucial for differentiating them from oncogenic RNA tumor viruses.
Purpose of the Study:
- To elucidate the unique structural properties of isolated murine intracisternal A particles.
- To compare the structural composition and stability of A particles with known oncogenic viruses.
Main Methods:
- Treatment of A particles with detergents (deoxycholate, Triton X-100) and sodium dodecyl sulfate (SDS).
- Analysis of structural integrity and protein solubilization.
- Characterization of major structural proteins by molecular weight.
Main Results:
- A particles exhibit a two-shell concentric structure.
- The outer shell shows partial susceptibility to detergents, while the inner shell is detergent-resistant.
- Disulfide bonding stabilizes the inner shell proteins, including a major ~70,000 MW protein.
- A ~80,000 MW protein may be involved in inner-outer shell attachment.
Conclusions:
- Murine intracisternal A particles possess a unique, stabilized structure distinct from oncogenic RNA tumor viruses.
- Disulfide bonds play a critical role in the structural integrity of the A particle inner shell.
- Specific protein components contribute to the distinct structural organization of A particles.