Figures
Herpes viral adaptor protein HSV-1 ICP27 recognizes and specifically binds to the surface of the RRM domain of cellular export factor REF/Aly.
The recognition fragment of the ICP27 peptide is shown docked to the binding pocket on the REF RRM, with selected residues labeled. A similar binding surface on REF/Aly is occupied by an adaptor protein from a different herpesvirus, HVS ORF57. The importance of the key amino acid residues within the binding sites of both viral proteins was confirmed by site-directed mutagenesis. Together, these data precisely map amino acid residues responsible for the direct interactions between viral adaptors and cellular REF/Aly and provide the first molecular details of how herpes viruses access the cellular mRNA export pathway (see Tunnicliffe et al., doi:10.1371/journal.ppat.1001244).
Image Credit: Richard B. Tunnicliffe and Alexander P. Golovanov, University of Manchester
Citation: (2011) PLoS Pathogens Issue Image | Vol. 7(1) January 2011. PLoS Pathog 7(1): ev07.i01. https://doi.org/10.1371/image.ppat.v07.i01
Published: January 27, 2011
Copyright: © 2011 Tunnicliffe, Golovanov. 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 recognition fragment of the ICP27 peptide is shown docked to the binding pocket on the REF RRM, with selected residues labeled. A similar binding surface on REF/Aly is occupied by an adaptor protein from a different herpesvirus, HVS ORF57. The importance of the key amino acid residues within the binding sites of both viral proteins was confirmed by site-directed mutagenesis. Together, these data precisely map amino acid residues responsible for the direct interactions between viral adaptors and cellular REF/Aly and provide the first molecular details of how herpes viruses access the cellular mRNA export pathway (see Tunnicliffe et al., doi:10.1371/journal.ppat.1001244).
Image Credit: Richard B. Tunnicliffe and Alexander P. Golovanov, University of Manchester