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Two Epstein-Barr virus-associated DNA polymerase activities.

S R Goodman, C Prezyna, W C Benz

    The Journal of Biological Chemistry
    |December 10, 1978
    PubMed
    Summary
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    Researchers identified two distinct DNA polymerase activities linked to Epstein-Barr virus (EBV). One is EBV-induced, the other virion-associated, differing in purification, salt resistance, pH optima, and template usage.

    Area of Science:

    • Virology
    • Molecular Biology
    • Enzymology

    Background:

    • Epstein-Barr virus (EBV) is a human herpesvirus implicated in various diseases.
    • DNA polymerases are crucial for viral replication and cellular processes.
    • Understanding EBV-associated enzymes is key to deciphering its lifecycle.

    Purpose of the Study:

    • To partially purify and characterize DNA polymerase activities associated with EBV.
    • To differentiate EBV-induced and EBV virion-associated DNA polymerases from host enzymes.
    • To investigate the biochemical properties and substrate specificities of these viral polymerases.

    Main Methods:

    • Partial purification of DNA polymerase activities using ion-exchange chromatography (DEAE-cellulose, phosphocellulose) and glycerol gradient sedimentation.

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  • Enzyme characterization including salt inhibition, pH optima, substrate saturation kinetics, and primer-template utilization.
  • Distinguishing viral polymerases from host DNA polymerases (alpha, beta, gamma) and reverse transcriptase.

    • Main Results:

    • Two distinct DNA polymerase activities were identified: EBV-induced and EBV virion-associated.
    • The EBV-induced polymerase showed salt resistance, a basic pH optimum (9.5), and high affinity for activated DNA.
    • The EBV virion-associated polymerase exhibited unique template preferences and was distinguished by its inability to efficiently copy ribohomopolymers.

    Conclusions:

    • Epstein-Barr virus encodes or induces at least two distinct DNA polymerase activities.
    • These viral polymerases possess unique biochemical properties differentiating them from host polymerases.
    • The characterized enzymes are potential targets for antiviral therapies against EBV.