November 1, 1983Journal of VirologyOpen Access

Antibody to a synthetic nonapeptide corresponding to the NH2 terminus of poliovirus genome-linked protein VPg reacts with native VPg and inhibits in vitro replication of poliovirus RNA

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Structured PICO

Population

In vitro model of poliovirus RNA replication and rabbits used to raise antibodies

Intervention

Antipeptide antibodies raised against a synthetic nonapeptide corresponding to the N-terminal sequence of poliovirus genome-linked protein (VPg)

Comparator

Preincubation of antibodies with excess nonapeptide; oligouridylic acid-stimulated RNA synthesis

Outcome

Inhibition of host factor-stimulated, poliovirus replicase-catalyzed in vitro synthesis of full-length (35S) RNAsurrogate

Antibodies targeting the N-terminus of poliovirus VPg inhibit in vitro replication of poliovirus RNA, indicating a functional role for VPg in viral genome replication.

Discussion

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Implication

Hypothesis-generating for VPg as antiviral target; leaves open in vivo efficacy and clinical translation.

Cite This Study

Morrow et al. (1983) studied this question.

synapsesocial.com/papers/6a87d3f1f8efd6d7e4fb1854 https://doi.org/10.1128/jvi.48.2.429-439.1983

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Antibody to a synthetic nonapeptide corresponding to the NH2 terminus of poliovirus genome-linked protein VPg reacts with native VPg and inhibits in vitro replication of poliovirus RNA

Structured PICO

Discussion

Implication

Cite This Study

Antibody to a synthetic nonapeptide corresponding to the NH2 terminus of poliovirus genome-linked protein VPg reacts with native VPg and inhibits in vitro replication of poliovirus RNA

Structured PICO

Discussion

Implication

Cite This Study

Also Consider

Also Consider