Abstract
Development of novel strategies targeting the highly virulent ebolaviruses is urgently required. A proteomic study identified the ER chaperone HSPA5 as an ebolavirus-associated host protein. Here, we show using the HSPA5 inhibitor (-)- epigallocatechin gallate (EGCG) that the chaperone is essential for virus infection, thereby demonstrating a functional significance for the association. Furthermore, in vitro and in vivo gene targeting impaired viral replication and protected animals in a lethal infection model. These findings demonstrate that HSPA5 is vital for replication and can serve as a viable target for the design of host-based countermeasures.
Original language | English (US) |
---|---|
Pages (from-to) | 171-174 |
Number of pages | 4 |
Journal | Antiviral Research |
Volume | 109 |
Issue number | 1 |
DOIs | |
State | Published - Sep 2014 |
Externally published | Yes |
Keywords
- Antiviral
- Ebolavirus
- HSPA5
ASJC Scopus subject areas
- Pharmacology
- Virology