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The respiratory syncytial virus (RSV) RNA polymerase is a multifunctional enzyme complex essential for the transcription and replication of the RSV genome. RSV is a nonsegmented, negative-sense RNA virus, and its polymerase complex orchestrates both mRNA synthesis (transcription) and genome replication. The core of the RSV polymerase complex consists of the L protein (Large protein) which functions as an RNA-dependent RNA polymerase (RdRp), catalyzing nucleotide polymerization, mRNA capping, and cap methylation, and the P protein (Phosphoprotein) which acts as an essential cofactor for L and recruits other proteins necessary for efficient transcription/replication. Additional components include the nucleoprotein (N) which encapsidates viral genomic RNA and the M2-1 protein which serves as a processivity factor required for efficient transcription. Small-molecule inhibitors targeting various functions/domains within this enzyme have shown antiviral efficacy in vitro/in vivo models, making it a valuable antiviral drug target against RSV infection.
Inhibition of RNA-dependent RNA polymerase activity, inhibition of mRNA capping/methylation
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