{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["94(13)"],"submitter":["Medina GN"],"funding":["U.S. Department of Agriculture"],"pubmed_abstract":["Foot-and-mouth disease virus (FMDV) leader proteinase (Lpro) affects several pathways of the host innate immune response. Previous studies in bovine cells demonstrated that deletions (leaderless [LLV]) or point mutations in Lpro result in increased expression of interferon (IFN) and IFN-stimulated genes (ISGs), including, among others, the ubiquitin-like protein modifier ISG15 and the ubiquitin specific peptidase USP18. In addition to its conventional papain-like protease activity, Lpro acts as a deubiquitinase (DUB) and deISGylase. In this study, we identified a conserved residue in Lpro that is involved in its interaction with ISG15. Mutation W105A rendered Escherichia coli-expressed Lpro unable to cleave the synthetic substrate pro-ISG15 while preserving cellular eIF4G cleavage. Interes"],"journal":["Journal of virology"],"pagination":["e00341-20"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7307143"],"repository":["biostudies-literature"],"pubmed_title":["Impairment of the DeISGylation Activity of Foot-and-Mouth Disease Virus Lpro Causes Attenuation In Vitro and In Vivo."],"pmcid":["PMC7307143"],"pubmed_authors":["Ramirez-Medina E","Fang Y","Gutkoska J","Medina GN","Diaz-San Segundo F","de Los Santos T","Azzinaro P"],"additional_accession":[]},"is_claimable":false,"name":"Impairment of the DeISGylation Activity of Foot-and-Mouth Disease Virus Lpro Causes Attenuation In Vitro and In Vivo.","description":"Foot-and-mouth disease virus (FMDV) leader proteinase (Lpro) affects several pathways of the host innate immune response. Previous studies in bovine cells demonstrated that deletions (leaderless [LLV]) or point mutations in Lpro result in increased expression of interferon (IFN) and IFN-stimulated genes (ISGs), including, among others, the ubiquitin-like protein modifier ISG15 and the ubiquitin specific peptidase USP18. In addition to its conventional papain-like protease activity, Lpro acts as a deubiquitinase (DUB) and deISGylase. In this study, we identified a conserved residue in Lpro that is involved in its interaction with ISG15. Mutation W105A rendered Escherichia coli-expressed Lpro unable to cleave the synthetic substrate pro-ISG15 while preserving cellular eIF4G cleavage. Interes","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Jun","modification":"2025-04-29T10:51:51.79Z","creation":"2020-11-09T08:47:18Z"},"accession":"S-EPMC7307143","cross_references":{"pubmed":["32295921"],"doi":["10.1128/JVI.00341-20"]}}