Abstract:
:Human cytomegalovirus terminase complex cleaves the concatemeric genomic viral DNA into unit lengths during genome packaging and particle assembly. Terminase complex ATPase and endonuclease activity is provided by the viral protein pUL89. pUL89 is an attractive drug target because its activities are required for infectious virus production. A domain located in the C-terminus of pUL89 has an RNase H/integrase-like fold and endonuclease activity that can be inhibited by compounds featuring a chelating triad motif. Previously, we developed a novel ELISA approach to screen for pUL89 inhibitors. In this report, we used the ELISA to identify 3-hydroxypyrimidine-2,4-dione as a promising scaffold for pUL89 inhibitor development. Several potent pUL89 inhibitors yielded low micromolar IC50 values in the enzymatic assay and low micromolar EC50 values for inhibition of HCMV replication. Two representative compounds inhibitory effects depended upon metal ions and occurred late in virus replication consistent with pUL89 inhibitors in infected cells.
journal_name
Antiviral Resjournal_title
Antiviral researchauthors
Wang Y,Tang J,Wang Z,Geraghty RJdoi
10.1016/j.antiviral.2018.01.015subject
Has Abstractpub_date
2018-04-01 00:00:00pages
10-17eissn
0166-3542issn
1872-9096pii
S0166-3542(17)30692-7journal_volume
152pub_type
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