Abstract
Ubiquitination is an important post-translational modification (PTM) that plays a key role in almost every aspect of cellular processes and many signaling pathways in eukaryotes. In this study, we performed a quantitative ubiquitome study to identify the global change of ubiquitination induced by rabies virus (RABV) infection in the mouse brain tissue. 4,243 ubiquitinated sites, mapping to 1,626 proteins were identified; using a cutoff of fold change >2, 644 and 70 ubiquitinated proteins were up- and down-regulated, respectively. GO analysis indicated that the differentially ubiquitinated proteins (DUPs) were significantly enriched in the myelin sheath of cells and binding activity. KEGG pathway analysis indicated that the identified proteins were related to biosynthesis of amino acids. Of note, ubiquitination was observed on all five RABV proteins by both proteomics and biochemical approaches. Our study revealed the global ubiquitome of RABV-infected mice and provides a valuable resource for investigating the pathogenic mechanisms of RABV.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
