The presence of cellular factors that bind to the 3' untranslated region (UTR) of picornaviruses was investigated by electrophoretic mobility shift assays (EMSAs). A cellular factor(s) that binds specifically the 3' UTR of polio-, coxsackie- and rhinoviruses was detected. Furthermore, this factor(s) is distinct from those which bind to the 5' terminal 88 nt (the 'cloverleaf') of poliovirus. Mutations within the 3' UTR which decrease the affinity of the RNA for the cellular factor in EMSAs decrease RNA replication and virus viability. Revertants of these mutants display changes which are predicted to stabilize the RNA secondary structure of the 3' UTR. These results indicate that binding of a cellular factor to the UTR plays a role in virus replication and that RNA secondary structure is important for this function.


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