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Structural polypeptides of simian virus 40.

M K Estes, E S Huang, J S Pagano

    Journal of Virology
    |May 1, 1971
    PubMed
    Summary
    This summary is machine-generated.

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    Simian virus 40 (SV40) structural polypeptides were identified using SDS-PAGE, revealing six distinct proteins (VP1-VP6) with varying molecular weights and ratios. VP1 and VP2 likely form the capsid, while VP4-VP6 associate with DNA.

    Area of Science:

    • Virology
    • Molecular Biology
    • Biochemistry

    Background:

    • Simian virus 40 (SV40) is a well-characterized DNA tumor virus.
    • Understanding SV40's structural components is crucial for comprehending its replication and assembly.

    Purpose of the Study:

    • To identify and characterize the structural polypeptides of simian virus 40.
    • To determine the molecular weights and relative abundance of these viral proteins.

    Main Methods:

    • Purified SV40 virions were analyzed using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).
    • Radioactive labeling and protein staining techniques were employed for visualization and quantification.
    • Velocity centrifugation in sucrose gradients was used to study polypeptide-DNA interactions.

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    Main Results:

    • Six distinct polypeptides (VP1-VP6) were identified with approximate molecular weights: VP1 (43,000 Da), VP2 (32,000 Da), VP3 (23,000 Da), VP4 (14,000 Da), VP5 (12,500 Da), and VP6 (11,000 Da).
    • VP1 constituted the major virion protein (70%), suggesting a primary role in capsid formation.
    • VP1 and VP2 remained associated with the capsid structure, while VP4, VP5, and VP6 complexed with viral DNA upon degradation.

    Conclusions:

    • The structural analysis revealed a complex protein composition for SV40.
    • VP1 and VP2 are proposed to form the major capsid proteins.
    • Smaller polypeptides (VP4-VP6) likely form a nucleoprotein complex with viral DNA, with VP3 acting as a potential intermediate.