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Abraham lab at Harvard Medical School @abrahamlabhms.bsky.social · 16/09/2026

The structures reveal that after binding to the polymerase, a conformational change in the E5 helicase-primase exposes the helicase ssDNA channel, activating the helicase. Single-molecule optical tweezers experiments done with @joeloparo.bsky.social confirmed this activation mechanism.

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Abraham lab at Harvard Medical School @abrahamlabhms.bsky.social · 16/09/2026

We further determined a structure of the primase-polymerase core complex in a state that likely occurs during the synthesis of RNA primers.

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Abraham lab at Harvard Medical School @abrahamlabhms.bsky.social · 16/09/2026

Taken together, our work provides a mechanism for MPXV replisome assembly and E5 helicase-primase activation in viral DNA replication. These findings may provide valuable targets for antiviral therapy development that may lock 🔒 the replisome in conformational intermediates.

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