Please use this identifier to cite or link to this item: https://doi.org/10.1128/JVI.01078-16
Title: ITCH E3 ubiquitin ligase interacts with Ebola virus VP40 to regulate budding
Authors: Han, Z
Sagum, C.A
Bedford, M.T
Sidhu, S.S
Sudol, M 
Harty, R.N
Keywords: protein VP40
ubiquitin protein ligase
ubiquitin protein ligase ITCH E3
ubiquitin protein ligase NEDD4
unclassified drug
core protein
ITCH protein, human
nucleoprotein
nucleoprotein VP40, Ebola virus
repressor protein
ubiquitin protein ligase
Article
controlled study
Ebolavirus
enzyme activation
enzyme activity
human
human cell
nonhuman
priority journal
protein binding
protein domain
protein expression
protein function
protein interaction
regulatory mechanism
virion
virus particle
virus release
animal
cell line
Ebolavirus
host pathogen interaction
metabolism
physiology
protein analysis
Animals
Cell Line
Ebolavirus
Host-Pathogen Interactions
Humans
Nucleoproteins
Protein Interaction Mapping
Repressor Proteins
Ubiquitin-Protein Ligases
Viral Core Proteins
Virus Release
Issue Date: 2016
Publisher: American Society for Microbiology
Citation: Han, Z, Sagum, C.A, Bedford, M.T, Sidhu, S.S, Sudol, M, Harty, R.N (2016). ITCH E3 ubiquitin ligase interacts with Ebola virus VP40 to regulate budding. Journal of Virology 90 (20) : 9163-9171. ScholarBank@NUS Repository. https://doi.org/10.1128/JVI.01078-16
Abstract: Ebola virus (EBOV) and Marburg virus (MARV) belong to the Filoviridae family and can cause outbreaks of severe hemorrhagic fever, with high mortality rates in humans. The EBOV VP40 (eVP40) and MARV VP40 (mVP40) matrix proteins play a central role in virion assembly and egress, such that independent expression of VP40 leads to the production and egress of virus-like particles (VLPs) that accurately mimic the budding of infectious virus. Late (L) budding domains of eVP40 recruit host proteins (e.g., Tsg101, Nedd4, and Alix) that are important for efficient virus egress and spread. For example, the PPxY-type L domain of eVP40 and mVP40 recruits the host Nedd4 E3 ubiquitin ligase via itsWWdomains to facilitate budding. Here we sought to identify additionalWWdomain host interactors and demonstrate that the PPxY L domain motif of eVP40 interacts specifically with theWWdomain of the host E3 ubiquitin ligase ITCH. ITCH, like Nedd4, is a member of the HECT class of E3 ubiquitin ligases, and the resultant physical and functional interaction with eVP40 facilitates VLP and virus budding. Identification of this novel eVP40 interactor highlights the functional interplay between cellular E3 ligases, ubiquitination, and regulation of VP40-mediated egress. © 2016, American Society for Microbiology.
Source Title: Journal of Virology
URI: https://scholarbank.nus.edu.sg/handle/10635/175267
ISSN: 0022-538X
DOI: 10.1128/JVI.01078-16
Appears in Collections:Staff Publications
Elements

Show full item record
Files in This Item:
File Description SizeFormatAccess SettingsVersion 
10_1128_JVI_01078-16.pdf968.29 kBAdobe PDF

OPEN

NoneView/Download

SCOPUSTM   
Citations

21
checked on Oct 19, 2020

Page view(s)

7
checked on Oct 22, 2020

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.