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The Connector Domain of Vesicular Stomatitis Virus Large Protein Interacts with the Viral Phosphoprotein

J Virol. 2020; 
Gould JR, Qiu S, Shang Q, Ogino T, Prevelige PE Jr, Petit CM, Green TJ
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Peptide Synthesis Peptides comprising VSV P residues 76-106, 80-106, or 95-106 with the 341 sequence N-VPDPEAEQVEGFIQGPLDDYADEDVDVVFTS, N- on January 7, 2020 at TULANE UNIV http://jvi.asm.org/ Downloaded from 16 EAEQVEGFIQGPLDDYADEDVDVVFTS, or N-YADEDVDVVFTS respectively were synthesized by GenScript (Piscataway, NJ) both with and without an N-terminal Fluorescein isothiocyanate (FITC) label. Get A Quote

摘要

Vesicular stomatitis virus (VSV) is an archetypical member of Mononegavirales, viruses with a genome of negative-sense single-stranded RNA (-ssRNA). Like other viruses of this order, VSV encodes a unique polymerase, a complex of viral L (large, the enzymatic component) protein and P (phosphoprotein, a cofactor component). The L protein has a modular layout consisting of a ring-shaped core trailed by three accessory domains and requires an N-terminal segment of P (P N-terminal disordered [PNTD]) to perform polymerase activity. To date, a binding site for P on L had not been described. In this report, we show that the connector domain of the L protein, which previously had no assigned function, binds a component ... More

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