Conserved herpesvirus protein kinase (CHPK)-mediated phosphorylation of viral proteins associated with nucleocytoplasmic trafficking during natural infection
Analysis of viral gene expression, protein abundance, and post-translational modifications (PTMs) during natural infection suggests that MDV CHPK orchestrates the subcellular localization of multiple viral proteins in epithelial skin cells via phosphorylation, thereby enabling efficient replication and horizontal transmission in the natural host.
The results show that nucleocytoplasmic shuttling of UL47_TEG5 is mediated through a non-canonical mechanism and highlight UL47_TEG5 as a potential target for improved vaccines to better control this economically important disease.
A high-resolution map of host-driven PTMs on ZIKV proteins as well as cellular interacting kinases are defined, novel mechanisms of host driven-regulation of ZIKV particle release and cytopathogenicity are uncovered, and an FDA-approved inhibitor of ZIKV growth is identified.
I. Manuelyan, Anna M. Schmoker, B. Yount et al.· PLoS Pathogens· 0 citations
The existing mechanistic knowledge about the PTBP1 functions during viral infection is described and the possibility of PTBP1 being used as a host-directed antiviral drug target despite the hurdles in doing so considering its multifunctionality as an essential cellular RNA-binding protein is explored.
A novel strategy by which Kaposi’s sarcoma-associated herpesvirus hijacks RNA-mediated signaling to support its lifecycle is revealed, highlighting the essential role of RNA interactions in viral gene regulation and pathogenesis.
Yang Zhao, Xiang Ye, Madeline Yuen et al.· Nature Communications· 0 citations
This work observed that the NS5 protein of tick-borne encephalitis virus (TBEV) localized both in the cytoplasm and nucleoplasm of infected human cells and identified the specific residues responsible for its nuclear addressing and showed that it interacts with numerous nuclear proteins, including some involved in regu...
Maxime Chazal, A. Sow, Elodie le Seac'h et al.· Journal of Virology· 0 citations
Using recombinant viruses generated in this study, the effects of the K247 ubiquitination site on host cell metabolism are investigated and indicate that the K247 residue of the NDV M protein enhances viral budding and promotes rapid utilization of host sphingolipids.
Jun Dai, Fan-Xin Liu, Yiyi Feng et al.· Poultry Science· 0 citations
We use cookies to run the site and, with your consent, for analytics and to show ads.
See our Cookie Policy.
