Key result
The connector domain of the vesicular stomatitis virus large protein directly interacts with the viral phosphoprotein, and this interaction is a positive regulator of viral RNA synthesis.
The study identifies the connector domain of the VSV L protein as the binding site for the viral phosphoprotein, providing a potential target for antiviral development against negative-strand RNA viruses.
Identifies a novel mechanistic target for antiviral drug development; leaves open whether disrupting this specific protein-.
This study represents the first functional assignment of the connector domain of a Mononegavirales L protein. Furthermore, this study localizes P polymerase cofactor activity to specific amino acids. The functional necessity of this interaction, combined with the uniqueness of L and P proteins to the order Mononegavirales , makes disruption of the P-connector site a potential target for developing antivirals against other negative-strand RNA viruses. Furthermore, the connector domain as an acceptor site for the P protein represents a new understanding of Mononegavirales L protein biology.
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Gould et al. (2020) studied Vesicular stomatitis virus (in vitro). Mutagenesis of VSV L and P proteins vs. Wild-type proteins was evaluated on Viral RNA synthesis (minigenome reporter activity). The connector domain of the vesicular stomatitis virus large protein directly interacts with the viral phosphoprotein, and this interaction is a positive regulator of viral RNA synthesis.
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