| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5822202 | Antiviral Research | 2014 | 4 Pages |
â¢Targeting HSPA5 chaperone activity inhibits EBOV.â¢EBOV transcript and protein production is impaired in the absence of HSPA5.â¢Targeting HSPA5 in vivo protects mice from lethal EBOV.
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.
