Figures
Targeting of the respiratory syncytial transcription factor M2-1 to viral inclusion bodies revealed by NMR and site-directed mutagenesis.
The respiratory syncytial virus (RSV) RNA-dependent RNA polymerase machinery is localized in cytoplasmic inclusion bodies (IBs), which are regarded as sites of viral RNA synthesis. The RSV transcription factor M2-1 is targeted to these IBs by interacting with the phosphoprotein, the main RNA polymerase cofactor. This interaction is mediated by the “core” domain of M2-1 (See Blondot et al., doi:10.1371/journal.ppat.1002734). The structure of this domain was solved by NMR, and residues involved in the P-M2-1 interaction were revealed. Mutagenesis of these residues on M2-1 (labeled in green) excluded it from IBs where P is still localized (labeled in red).
Image Credit: Marie-Lise Blondot and Jean-François Éléouët, INRA
Citation: (2012) PLoS Pathogens Issue Image | Vol. 8(5) May 2012. PLoS Pathog 8(5): ev08.i05. https://doi.org/10.1371/image.ppat.v08.i05
Published: May 31, 2012
Copyright: © 2012 Blondot. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
The respiratory syncytial virus (RSV) RNA-dependent RNA polymerase machinery is localized in cytoplasmic inclusion bodies (IBs), which are regarded as sites of viral RNA synthesis. The RSV transcription factor M2-1 is targeted to these IBs by interacting with the phosphoprotein, the main RNA polymerase cofactor. This interaction is mediated by the “core” domain of M2-1 (See Blondot et al., doi:10.1371/journal.ppat.1002734). The structure of this domain was solved by NMR, and residues involved in the P-M2-1 interaction were revealed. Mutagenesis of these residues on M2-1 (labeled in green) excluded it from IBs where P is still localized (labeled in red).
Image Credit: Marie-Lise Blondot and Jean-François Éléouët, INRA