Journal
VETERINARY RESEARCH
Volume 46, Issue -, Pages -Publisher
BMC
DOI: 10.1186/s13567-015-0273-1
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Funding
- National Natural Sciences Foundation of China [31302118, 31502042, 31402179]
- Gansu Science Foundation for Distinguished Young Scholars [145RJDA328]
- International Atomic Energy Agency [16025/R0]
- National Science and Technology Ministry [2015BD12B04]
- Key technologies R&D program of Gansu Province [1302NKDA027]
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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 gamma (eIF4G) to shut off host protein synthesis; (2) inhibition of host innate immune responses through restriction of interferon-alpha/beta 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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