AUTHOR=Azzinaro Paul A. , Medina Gisselle N. , Rai Devendra , Ramirez-Medina Elizabeth , Spinard Edward , Rodriguez-Calzada Monica , Zhu James , Rieder Elizabeth , de los Santos Teresa , Díaz-San Segundo Fayna TITLE=Mutation of FMDV Lpro H138 residue drives viral attenuation in cell culture and in vivo in swine JOURNAL=Frontiers in Veterinary Science VOLUME=9 YEAR=2022 URL=https://www.frontiersin.org/journals/veterinary-science/articles/10.3389/fvets.2022.1028077 DOI=10.3389/fvets.2022.1028077 ISSN=2297-1769 ABSTRACT=
The foot-and-mouth disease virus (FMDV) leader proteinase (Lpro) is a papain like protease that cleaves the viral polyprotein and several host factors affecting host cell translation and induction of innate immunity. Introduction of Lpro mutations ablating catalytic activity is not tolerated by the virus, however, complete coding sequence deletion or introduction of targeted amino acid substitutions can render viable progeny. In proof-of-concept studies, we have previously identified and characterized FMDV Lpro mutants that are attenuated in cell culture and in animals, while retaining their capacity for inducing a strong adaptive immunity. By using molecular modeling, we have now identified a His residue (H138), that resides outside the substrate binding and catalytic domain, and is highly conserved across serotypes. Mutation of H138 renders possible FMDV variants of reduced virulence