Key result
Foot-and-mouth disease virus leader protein (Lpro) suppresses host antiviral responses by cleaving eIF4G, inhibiting interferon production, and acting as a deubiquitinase.
This review summarizes the mechanisms by which the FMDV leader protein antagonizes host antiviral responses to promote viral replication.
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May guide FMDV antiviral strategies; leaves open in vivo validation in livestock.
Foot-and-mouth disease virus (FMDV) leader protein (L(pro)) is a papain-like proteinase, which plays an important role in FMDV pathogenesis. L(pro) exists as two forms, Lab and Lb, due to translation being initiated from two different start codons separated by 84 nucleotides. L(pro) self-cleaves from the nascent viral polyprotein precursor as the first mature viral protein. In addition to its role as a viral proteinase, L(pro) also has the ability to antagonize host antiviral effects. To promote FMDV replication, L(pro) can suppress host antiviral responses by three different mechanisms: (1) cleavage of eukaryotic translation initiation factor 4 γ (eIF4G) to shut off host protein synthesis; (2) inhibition of host innate immune responses through restriction of interferon-α/β production; and (3) L(pro) can also act as a deubiquitinase and catalyze deubiquitination of innate immune signaling molecules. In the light of recent functional and biochemical findings regarding L(pro), this review introduces the basic properties of L(pro) and the mechanisms by which it antagonizes host antiviral responses.
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Liu et al. (2015) conducted a review in Foot-and-mouth disease virus (FMDV) infection. FMDV leader protein (Lpro) was evaluated. Foot-and-mouth disease virus leader protein (Lpro) suppresses host antiviral responses by cleaving eIF4G, inhibiting interferon production, and acting as a deubiquitinase.
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