Affiliation:
1. Institut für Virologie, Philipps-Universität Marburg, Marburg, Germany
2. Laboratory of Ultrastructural Virology, Institute for Frontier Life and Medical Sciences, Kyoto University, Kyoto, Japan
3. German Center of Infection Research (DZIF), Partner Site Giessen-Marburg-Langen, Marburg, Germany
Abstract
Ebola virus (EBOV) causes a severe fever with high case fatality rates and, so far, no available specific therapy. Understanding the interplay between viral and host proteins is important to identify new therapeutic approaches. VP24 is one of the essential nucleocapsid components and is necessary to regulate viral RNA synthesis and condense viral nucleocapsids before their transport to the plasma membrane. Our functional analyses of the YxxL motif in VP24 suggested that it serves as an interface between nucleocapsid-like structures (NCLSs) and cellular proteins, promoting intracellular transport of NCLSs in an Alix-independent manner. Moreover, the YxxL motif is necessary for the inhibitory function of VP24 in viral RNA synthesis. A failure to rescue EBOV encoding VP24 with a mutated YxxL motif indicated that the integrity of the YxxL motif is essential for EBOV growth. Thus, this motif might represent a potential target for antiviral interference.
Funder
Institute for Frontier Life and Medical Sciences Kyoto University
The Ichiro Kanahara Foundation
Deutsche Forschungsgemeinschaft
Takeda Science Foundation
Daiichi Sankyo Foundation of Life Science
Uehara Memorial Foundation
Japan Agency for Medical Research and Development
University of Tokyo
MEXT | Japan Society for the Promotion of Science
Publisher
American Society for Microbiology
Subject
Virology,Insect Science,Immunology,Microbiology
Cited by
10 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献