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• W2791233348 startingPage "139" @default.
• W2791233348 abstract "Cardioviruses cause diseases in many animals including, in rare cases, humans. Although they share common features with all picornaviruses, cardioviruses have unique properties that distinguish them from other family members, including enteroviruses. One feature shared by all picornaviruses is the covalent attachment of VPg to the 5' end of genomic RNA via a phosphotyrosyl linkage. For enteroviruses, this linkage is cleaved by a host cell protein, TDP2. Since TDP2 is divergently required during enterovirus infections, we determined if TDP2 is necessary during infection by the prototype cardiovirus, EMCV. We found that EMCV yields are reduced in the absence of TDP2. We observed a decrease in viral protein accumulation and viral RNA replication in the absence of TDP2. In contrast to enterovirus infections, we found that TDP2 is modified at peak times of EMCV infection. This finding suggests a unique mechanism for cardioviruses to regulate TDP2 activity during infection." @default.
• W2791233348 created "2018-03-29" @default.
• W2791233348 creator A5044053330 @default.
• W2791233348 creator A5063519792 @default.
• W2791233348 creator A5074722957 @default.
• W2791233348 date "2018-03-01" @default.
• W2791233348 modified "2023-09-29" @default.
• W2791233348 title "VPg unlinkase/TDP2 in cardiovirus infected cells: Re-localization and proteolytic cleavage" @default.
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• W2791233348 doi "https://doi.org/10.1016/j.virol.2018.01.010" @default.
• W2791233348 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5826889" @default.
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• W2791233348 hasPublicationYear "2018" @default.
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