title: The leader proteinase of foot-and-mouth disease virus: structure-function relationships in a proteolytic virulence factor.
abstract: The leader proteinase (Lpro) of the foot-and-mouth disease virus inhibits the host innate immune response by at least three different mechanisms. The most well-characterised of these is the prevention of the synthesis of cytokines such as interferons immediately after infection, brought about by specific proteolytic cleavage of the eukaryotic initiation factor 4G. This prevents the recruitment of capped cellular mRNA; however, the viral RNA can be translated under these conditions. The two other mechanisms are the induction of NF-κB cleavage and the deubiquitination of immune signalling molecules. This review focuses on the structure-function relationships in Lpro responsible for these widely divergent activities.
authors.forename: Jutta
authors.initials: J
authors.lastname: Steinberger
authors.forename: Tim
authors.initials: T
authors.lastname: Skern
mesh_terms: D000818:Animals; D029544:Foot-and-Mouth Disease Virus / Q000201:enzymology* / Q000235:genetics*; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D011500:Protein Synthesis Inhibitors; D012697:Serine Endopeptidases / Q000235:genetics / Q000378:metabolism*; D037521:Virulence Factors / Q000235:genetics* / Q000378:metabolism*
chemical_list: D008565:Membrane Proteins; D011500:Protein Synthesis Inhibitors; D037521:Virulence Factors; D012697:Serine Endopeptidases; C026515:type I signal peptidase