HSV for tumour lysis

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Interaction between the HCMV DNA polymerase subunits: toward a new antiviral target

Presented by A Loregian, University of Padova, Padova, Italy.

There is renewed interest in the search for novel human cytomegalovirus (HCMV) inhibitors, due to the emergence of drug-resistant virus strains, and because some antiviral agents currently used have toxic side-effects. The HCMV DNA polymerase represents a major target for antiviral chemotherapy. The HCMV DNA polymerase consists of a catalytic subunit, UL54, and an accessory protein, UL44, which is thought to stimulate the processivity of the enzyme. The recent observation that antisense inhibition of UL44 synthesis in HCMV-infected cells strongly inhibits viral DNA replication highlighted the importance of the accessory protein for virus growth, and raised the possibility that the UL54/UL44 interaction might be a valid target for antiviral drugs. To investigate this possibility, overlapping peptides spanning residues 1161 to 1242 of UL54 were synthesised and tested for inhibition of the interaction between UL54 and UL44. We identified a peptide, LPRRLHLEPAFLPYSVKAHECC, corresponding to residues 1221-1242 of UL54, which both disrupted the physical interaction between the two proteins and specifically inhibited the activity of the UL54/UL44 complex. The identification of a peptide that specifically inhibits DNA synthesis by HCMV DNA polymerase heralds the prospect that such a peptide, or shorter derivatives, could form the basis for the synthesis of peptidomimetics that inhibit HCMV replication.

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