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The Respiratory syncytial virus (RSV) matrix protein M2-1 is an essential transcription factor required for the viral life cycle. It functions as a transcription antitermination and processivity factor, enabling the viral RNA-dependent RNA polymerase to synthesize full-length mRNAs by preventing premature termination at gene junctions [2.2.1, 2.2.2]. M2-1 is a tetrameric RNA-binding protein that interacts with the viral phosphoprotein (P) and nucleoprotein (N) to facilitate the transition from transcription to replication [2.2.2, 2.4.3]. Because of its critical role in viral gene expression, M2-1 is considered a promising target for the development of small-molecule antivirals [2.2.1]. Experimental inhibitors like cyclopamine and triazole-1 have been shown to disrupt its function by targeting its RNA-binding domain or its interaction with the P protein [3.1.1, 3.2.1]. Additionally, M2-1 is utilized as an antigen in several viral-vectored vaccine candidates, such as PanAd3-RSV and MVA-RSV, to elicit cellular immune responses [2.1.1].
Inhibition of transcription antitermination and disruption of the interaction between M2-1 and the viral phosphoprotein (P) [3.1.1, 3.2.1].
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