Foot-and-mouth disease virus (FMDV) is a single-stranded, positive-sense RNA virus belonging to the genus Aphthovirus in the family Picornaviridae. FMDV enters cells via the mechanism of receptor-mediated endocytosis in which the low pH of the endosomal compartment triggers uncoating of the viral genome. FMDV enters cells by attaching itself to cellular receptor molecules of the integrin family. For FMDV the receptor has been identified as the Arg-Gly-Asp (RGD) binding integrin. The integrin-binding RGD is located in the G-H loop of VP1 and it is highly conserved among all seven serotypes. The FMDV genome organization is similar to that of other picornaviruses. The genome is composed of three parts, the 5’ non-translated region (5’NTR), the coding region and the 3’ non-translated region (3’NTR) containing a heteropolymeric segment and poly(A) tail, which is required for viral replication. The 5’NTR plays important roles in cap-independent translation initiation of the viral polyprotein and in viral genome replication. After translation, the polyprotein is cleaved into four primary cleavage products: the amino terminal L protease; P1-2A, the precursor of the capsid proteins; 2BC and P3 which are cleaved into nonstructural proteins.
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