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Related Concept Videos

Herpes01:28

Herpes

Herpes simplex type 1 (HSV‑1) is a widespread pathogen responsible for orolabial lesions. It is an enveloped, double-stranded DNA (dsDNA) virus belonging to the family Herpesviridae. Once the virus infects a host cell, its double‑stranded DNA genome is delivered into the nucleus, where a coordinated cascade of immediate‑early, early, and late gene expression directs viral DNA replication, structural protein synthesis, and virion assembly. After primary infection of epithelial cells, HSV-1...

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Related Experiment Video

Updated: Jun 4, 2026

Plaquing of Herpes Simplex Viruses
04:41

Plaquing of Herpes Simplex Viruses

Published on: November 5, 2021

Herpesvirus protease assays.

P Ertl, L Russell, J Angier

    Methods in Molecular Medicine
    |February 19, 2011
    PubMed
    Summary
    This summary is machine-generated.

    Herpesviruses use a serine protease for capsid maturation. This protease cleaves a polyprotein at specific sites, a process crucial for viral DNA packaging and a potential antiviral target.

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    Area of Science:

    • Virology
    • Structural Biology
    • Biochemistry

    Background:

    • Herpesviruses possess a serine protease critical for viral capsid maturation.
    • This protease is synthesized as part of a polyprotein, with a catalytic domain and a structural scaffold protein.
    • The scaffold protein is also expressed independently.

    Purpose of the Study:

    • To elucidate the function and structure of the herpesvirus serine protease and its scaffold protein.
    • To understand the cleavage mechanism of the polyprotein at the release (R) and maturation (M) sites.
    • To explore the potential of this protease as an antiviral target.

    Main Methods:

    • Analysis of polyprotein processing and cleavage sites.
    • Structural studies of the herpesvirus protease.
    • Investigating the role of protease cleavage in viral DNA packaging.

    Main Results:

    • The serine protease cleaves the polyprotein at the R-site (releasing the catalytic domain) and the M-site (maturation site).
    • M-site cleavage occurs post-procapsid assembly and is essential for viral DNA packaging.
    • The M-site sequence (V/L)-X-A-S is conserved across herpesviruses, with cleavage between A-S.
    • Herpesvirus proteases exhibit a novel structure.

    Conclusions:

    • The herpesvirus serine protease plays an indispensable role in viral capsid maturation through specific polyprotein cleavage.
    • The conserved M-site and novel protease structure highlight its significance as a potential target for antiviral drug development.