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The respiratory syncytial virus (RSV) RNA-dependent RNA polymerase (RdRp) is a multi-functional viral enzyme complex essential for the replication and transcription of the RSV genome. It is responsible for synthesizing both genomic and subgenomic RNAs from the negative-sense single-stranded viral RNA template. The core polymerase activity resides in the large L protein, which contains all enzymatic functions required for mRNA synthesis, capping, methylation, and polyadenylation. The L protein operates in conjunction with several cofactor proteins, including the phosphoprotein P, nucleoprotein N, and M2-1. It is an attractive antiviral target because it performs essential steps unique to virus replication not found in host cells. Both nucleoside analogs targeting active sites and non-nucleoside inhibitors interfering with allosteric functions have shown efficacy against this enzyme complex.
Inhibition of RNA polymerization, interference with RNA binding, disruption of RdRp complex formation
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