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Innate immune sensor LGP2 is cleaved by the Leader protease of foot-and-mouth disease virus

Fig 6

Mutation of the putative target sequence in LGP2 abolishes cleavage by Lbpro.

(A) Schematic representation of LGP2 showing the three subdomains in the conserved DExD/H helicase domain (Hel1, Hel2i and Hel2) and the C-terminal domain (CTD). The position and sequence of the conserved helicase motif VI (in red) and surrounding residues in the human and porcine proteins are indicated. Amino acid substitutions in the mutant version of hLGP2 (hLGP2MT) compared with WT sequence are indicated in the corresponding positions. (B) HEK293 cells were transfected with a plasmid encoding hLGP2-Myc-DDK (hLGP2WT) or its mutant version as indicated above (hLGP2MT) either alone or together with a plasmid encoding LbWT. The amount of DNA in all transfections was balanced with EV (-). Cell lysates were analyzed 24 h later by western blot for the indicated proteins using the specified antibodies. The N- and C-terminal cleavage products of LGP2 are indicated with arrows.

Fig 6