title: Identification of protein-protein interaction inhibitors targeting vaccinia virus processivity factor for development of antiviral agents.
abstract: Poxvirus uracil DNA glycosylase D4 in association with A20 and the catalytic subunit of DNA polymerase forms the processive polymerase complex. The binding of D4 and A20 is essential for processive polymerase activity. Using an AlphaScreen assay, we identified compounds that inhibit protein-protein interactions between D4 and A20. Effective interaction inhibitors exhibited both antiviral activity and binding to D4. These results suggest that novel antiviral agents that target the protein-protein interactions between D4 and A20 can be developed for the treatment of infections with poxviruses, including smallpox.
authors.affiliation: Department of Medicine, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA.
authors.forename: Norbert
authors.initials: N
authors.lastname: Schormann
authors.forename: Charnell Inglis
authors.initials: CI
authors.lastname: Sommers
authors.forename: Mark N
authors.initials: MN
authors.lastname: Prichard
authors.forename: Kathy A
authors.initials: KA
authors.lastname: Keith
authors.forename: James W
authors.initials: JW
authors.lastname: Noah
authors.forename: Manunya
authors.initials: M
authors.lastname: Nuth
authors.forename: Robert P
authors.initials: RP
authors.lastname: Ricciardi
authors.forename: Debasish
authors.initials: D
authors.lastname: Chattopadhyay
mesh_terms: D000998:Antiviral Agents / Q000494:pharmacology*; D002460:Cell Line; D045647:DNA Glycosylases / Q000378:metabolism; D006801:Humans; D011485:Protein Binding; D014616:Vaccinia virus / Q000187:drug effects*; D014764:Viral Proteins / Q000378:metabolism*
chemical_list: D000998:Antiviral Agents; D014764:Viral Proteins; D045647:DNA Glycosylases