Key result
Mutation of four surface residues on poliovirus polymerase decreased 3AB binding and 3B uridylylation, indicating that binding sites for the membrane tether and protein primer overlap.
The physical overlap of sites for protein priming and membrane association in poliovirus polymerase likely facilitates replication initiation in the membrane-associated complex.
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Surface residues may guide antiviral design; leaves open in vivo validation.
Lyle et al. (2002) studied this question. Mutational analysis of poliovirus polymerase vs. Wild-type poliovirus polymerase was evaluated on 3AB binding and 3B uridylylation. Mutation of four surface residues on poliovirus polymerase decreased 3AB binding and 3B uridylylation, indicating that binding sites for the membrane tether and protein primer overlap.
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