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Related Experiment Videos

Structural polypeptides of measles virus.

D L Tyrrell, E Norrby

    The Journal of General Virology
    |May 1, 1978
    PubMed
    Summary
    This summary is machine-generated.

    Measles virus structural proteins were analyzed, identifying six major polypeptides. The 79,000 MW polypeptide is likely the hemagglutinin, while the 40,000 MW protein may be involved in fusion.

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    Area of Science:

    • Virology
    • Molecular Biology
    • Biochemistry

    Background:

    • Measles virus is a significant human pathogen.
    • Understanding measles virus structure is crucial for developing antiviral strategies.

    Purpose of the Study:

    • To identify and characterize the structural polypeptides of measles virus.
    • To elucidate the function of identified viral proteins.

    Main Methods:

    • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was used to analyze viral polypeptides.
    • Radioactive labeling (3H-fucose, 3H-glucosamine, 35S-methionine) and enzymatic treatments (trypsin, galactose oxidase) were employed.

    Main Results:

    • Six major measles virus polypeptides were identified with molecular weights of 79,000, 72,000, 60,000, 43,000, 40,000, and 36,000.

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  • The 79,000 MW polypeptide was identified as the hemagglutinin.
  • The 40,000 MW polypeptide is likely involved in haemolysin and cell fusion activities.
  • A 43,000 MW polypeptide may represent incorporated cellular actin.

    • Conclusions:

    • The study successfully characterized key structural polypeptides of measles virus.
    • Identified proteins provide insights into measles virus entry and assembly mechanisms.