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This research aims to elucidate the structure and mechanism of the HSV-1 origin-binding protein UL9 in DNA replication.

July 12, 2026Journal of VirologyOpen Access

Structure and mechanism of the HSV-1 origin-binding protein UL9

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This research aims to elucidate the structure and mechanism of the HSV-1 origin-binding protein UL9 in DNA replication.
Utilized cryo-electron microscopy to obtain high-resolution structures of UL9 in apo and DNA-bound states.
Conducted biochemical and enzymatic assays to explore UL9's dimerization, origin recognition, and regulatory interactions with ICP8.
Identified UL9's stable homodimer formation crucial for origin binding.
Demonstrated UL9's interaction with ICP8 enhances DNA unwinding efficiency.
Highlighted structural insights that can inform antiviral drug design targeting viral replication.

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Randomized trial reveals the structure and function of UL9 in HSV-1, suggesting targets for antiviral drug development.

Huang et al. (2026) studied this question.

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