March 1, 1995Journal of VirologyOpen Access

Mutation of the aspartic acid residues of the GDD sequence motif of poliovirus RNA-dependent RNA polymerase results in enzymes with altered metal ion requirements for activity

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Structured PICO

Population

Poliovirus RNA-dependent RNA polymerase (3Dpol) expressed in Escherichia coli and tissue culture cells

Intervention

Oligonucleotide site-directed mutagenesis of the aspartic acids in the GDD motif of the 3Dpol gene and substitution of different metal ions (Mn2+, Fe2+, CoCl2)

Comparator

Wild-type 3Dpol enzyme and standard Mg2+ conditions

Outcome

In vitro poly(U) polymerase activity and poliovirus replication (production of infectious virus)surrogate

Mutations in the GDD motif of poliovirus RNA-dependent RNA polymerase alter its metal ion requirements for catalytic activity and viral replication.

Discussion

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Implication

Hypothesis-generating for metal-dependent viral polymerases; leaves open antiviral or vaccine applications in vivo.

Cite This Study

Jablonski et al. (1995) studied this question.

synapsesocial.com/papers/6a829339576c5bd0156d010f https://doi.org/10.1128/jvi.69.3.1532-1539.1995

View Full Paper

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Mutation of the aspartic acid residues of the GDD sequence motif of poliovirus RNA-dependent RNA polymerase results in enzymes with altered metal ion requirements for activity

Structured PICO

Discussion

Implication

Cite This Study

Mutation of the aspartic acid residues of the GDD sequence motif of poliovirus RNA-dependent RNA polymerase results in enzymes with altered metal ion requirements for activity

Structured PICO

Discussion

Implication

Cite This Study

Also Consider

Also Consider