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The leader proteinase of foot-and-mouth disease virus: structure-function relationships in a proteolytic virulence

Jutta Steinberger, Tim Skern

    Biological Chemistry
    |March 28, 2014
    PubMed

    Insights

    The foot-and-mouth disease virus leader proteinase (Lpro) suppresses host immunity via three mechanisms. Lpro cleaves host factors, preventing cytokine production and promoting viral translation, while also targeting immune signaling molecules.

    Area of Science:

    • Virology
    • Immunology
    • Molecular Biology

    Background:

    • Foot-and-mouth disease virus (FMDV) leader proteinase (Lpro) is crucial for viral replication.
    • Innate immune response is vital for host defense against viral infections.
    • Viruses often possess mechanisms to evade or suppress host immunity.

    Purpose of the Study:

    • To review the structure-function relationships of FMDV Lpro.
    • To elucidate the mechanisms by which Lpro inhibits the host innate immune response.
    • To understand how Lpro's structure enables its diverse functions.

    Main Methods:

    • Literature review of studies on FMDV Lpro.
    • Analysis of published data on Lpro's proteolytic activities.
    • Examination of Lpro's interactions with host factors.

    Main Results:

    • Lpro inhibits innate immunity through at least three distinct mechanisms.
    • Mechanism 1: Proteolytic cleavage of eukaryotic initiation factor 4G, inhibiting host mRNA translation and cytokine synthesis (e.g., interferons).
    • Mechanism 2 & 3: Induction of NF-κB cleavage and deubiquitination of immune signaling molecules.

    Conclusions:

    • FMDV Lpro possesses multiple strategies to counteract host innate immunity.
    • The structure of Lpro dictates its ability to perform diverse functions, including cleaving host factors and modulating immune signaling.
    • Understanding Lpro's structure-function relationship is key to developing antiviral strategies.

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