Figures
Co-localization of DENV NS5 with UBR4
Dengue virus (DENV) NS5 protein inhibits type I interferon signaling by mediating the proteasomal degradation of STAT2, which results in enhanced viral replication and dissemination in the host. Morrison et al. show that DENV NS5 protein interacts with UBR4, a member of a family of predicted E3 ligases. This interaction is critical for DENV NS5-mediated STAT2 degradation, and consequently for DENV replication, in the presence of a competent type I interferon system. This picture shows the co-localization of DENV NS5 with UBR4.
Image Credit: Giuseppe Pisanelli, Icahn School of Medicine at Mount Sinai, New York, NY, USA
Citation: (2013) PLoS Pathogens Issue Image | Vol. 9(3) March 2013. PLoS Pathog 9(3): ev09.i03. https://doi.org/10.1371/image.ppat.v09.i03
Published: March 28, 2013
Copyright: © 2013 Morrison et al. 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.
Dengue virus (DENV) NS5 protein inhibits type I interferon signaling by mediating the proteasomal degradation of STAT2, which results in enhanced viral replication and dissemination in the host. Morrison et al. show that DENV NS5 protein interacts with UBR4, a member of a family of predicted E3 ligases. This interaction is critical for DENV NS5-mediated STAT2 degradation, and consequently for DENV replication, in the presence of a competent type I interferon system. This picture shows the co-localization of DENV NS5 with UBR4.
Image Credit: Giuseppe Pisanelli, Icahn School of Medicine at Mount Sinai, New York, NY, USA