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Related Experiment Videos

Feline sarcoma virus-coded polyprotein: enzymatic cleavage by a type C virus-coded structural protein.

A S Khan, J R Stephenson

    Journal of Virology
    |February 1, 1979
    PubMed
    Summary

    A purified protein, p15, from Rous sarcoma virus enzymatically cleaves feline sarcoma virus polyprotein Pr130. This cleavage generates smaller proteins and isolates a 72,000 Mr nonstructural component.

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    Area of Science:

    • Virology
    • Molecular Biology
    • Biochemistry

    Background:

    • Rous sarcoma virus (RSV) is a retrovirus known to cause tumors in chickens.
    • Feline sarcoma virus (FeSV) is a replication-defective retrovirus that carries an oncogene.
    • Viral polyproteins are synthesized as large precursors that require proteolytic cleavage for maturation.

    Purpose of the Study:

    • To investigate the enzymatic activity of the RSV gag gene-coded protein p15.
    • To determine if p15 can cleave the FeSV-coded polyprotein Pr130.
    • To characterize the cleavage products of Pr130 and identify potential functional domains.

    Main Methods:

    • Purification of the 15,000-molecular-weight (Mr) Prague strain RSV gag gene-coded protein p15.
    • Enzymatic cleavage assays using purified p15 and FeSV-coded polyprotein Pr130.

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  • Analysis of cleavage products by molecular weight and protein purification.

    • Main Results:

    • Purified p15 enzymatically cleaved Pr130 into proteins ranging from 12,000 to 110,000 Mr.
    • p15 demonstrated specificity, as it did not significantly cleave other viral or nonviral proteins.
    • Feline leukemia virus Pr65gag was efficiently cleaved by p15, yielding p30, p15, p12, and p10.
    • A major 72,000 Mr cleavage product of Pr130 was purified and identified as containing a FeSV-coded nonstructural component.

    Conclusions:

    • The RSV p15 protein possesses specific enzymatic activity capable of cleaving FeSV polyproteins.
    • This cleavage process releases viral structural proteins and potentially exposes nonstructural components.
    • The findings contribute to understanding retroviral polyprotein processing and the generation of functional viral proteins.