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Characterization of a chimeric foot-and-mouth disease virus bearing a bovine rhinitis B virus leader proteinase

Sabena Uddowla, Juan M. Pacheco, Christopher Larson, Elizabeth Bishop, Luis L. Rodriguez, Devendra K. Rai, Jonathan Arzt, Elizabeth Rieder
Virology 2013 v.447 no.1-2 pp. 172-180
Bovine rhinitis B virus, Foot-and-mouth disease virus, aerosols, animal disease models, foot-and-mouth disease, host-pathogen relationships, hosts, immune response, in vivo studies, interferons, mutants, neutralization, neutralizing antibodies, pathogenesis, protein synthesis, proteinases, steers, swine, viral proteins, virulence, virus replication, viruses
Bovine rhinitis B virus (BRBV) shares many motifs and sequence similarities with foot-and-mouth disease virus (FMDV). This study examined if the BRBV leader proteinase (Lᵖʳᵒ) could functionally replace that of FMDV. A mutant A₂₄LBRV3DYR FMDV engineered with the BRBV Lᵖʳᵒ and an antigenic marker in the 3D polymerase exhibited growth properties and eIF4G cleavage similar to parental A₂₄WT virus. The A₂₄LBRV3DYR type I interferon activity in infected bovine cells resembled that of A₂₄LL virus that lacks Lᵖʳᵒ, but this effect was less pronounced for A₂₄LBRV3DYR infected porcine cells. In vivo studies showed that the A₂₄LBRV3DYR virus was attenuated in cattle, and exhibited low virulence in pigs exposed by direct contact. The mutant virus induced protective immunity in cattle against challenge with parental A₂₄WT. These results provide evidence that Lᵖʳᵒ of different Aphthoviruses are not fully functionally interchangeable and have roles that may depend on the nature of the infected host.