ArticleNucleic acids research2026
Structural insights into HSV-1 origin unwinding by the viral proteins UL9 and ICP8.
Article in Nucleic acids research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Herpes simplex virus type 1 (HSV-1) causes lifelong infections in human cells and is associated with a range of diseases. HSV-1 DNA replication requires seven viral proteins, including the major DNA-binding protein ICP8, the origin-binding protein UL9, and proteins that comprise the helicase-primase and DNA polymerase complexes. UL9 functions as a DNA helicase that specifically recognizes and binds to the viral origins of replication, OriS and OriL. Here we report the cryo-EM structure of the UL9/ICP8/DNA/ATPγS complex at an overall resolution of 3.18 Å. This structure revealed that UL9 employs an α-helix to separate the DNA strands and captures the initial step of OriS unwinding, in which the C-terminal domain of UL9 specifically binds to the major groove of a DNA double helix, while the N-terminal helicase domain engages the unwound leading and lagging strands. ICP8 interacts with the extreme C-terminal region of UL9, preventing UL9 dimerization. Simultaneously, it binds and stabilizes the leading-strand DNA adjacent to UL9. Together, these findings provide mechanistic insight into UL9-driven DNA unwinding and the cooperative action of UL9 and ICP8 at HSV-1 replication origins, establishing a structural framework for the rational interpretation of prior biochemical data and for the design of new antiviral drugs.
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