HSPA5 is an essential host factor for Ebola virus infection

St Patrick Reid; Amy C. Shurtleff; Julie A. Costantino; Sarah R. Tritsch; Cary Retterer; Kevin B. Spurgers; Sina Bavari

doi:10.1016/j.antiviral.2014.07.004

HSPA5 is an essential host factor for Ebola virus infection

St Patrick Reid, Amy C. Shurtleff, Julie A. Costantino, Sarah R. Tritsch, Cary Retterer, Kevin B. Spurgers, Sina Bavari

Research output: Contribution to journal › Article › peer-review

43 Scopus citations

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	https://doi.org/10.1016/j.antiviral.2014.07.004
State	Published - Sep 2014
Externally published	Yes

Keywords

Antiviral
Ebolavirus
HSPA5

ASJC Scopus subject areas

Pharmacology
Virology

Access to Document

10.1016/j.antiviral.2014.07.004

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title = "HSPA5 is an essential host factor for Ebola virus infection",

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.",

keywords = "Antiviral, Ebolavirus, HSPA5",

author = "{Patrick Reid}, St and Shurtleff, {Amy C.} and Costantino, {Julie A.} and Tritsch, {Sarah R.} and Cary Retterer and Spurgers, {Kevin B.} and Sina Bavari",

note = "Funding Information: We thank Sean Van Tongeren for performing mouse infections and Keren Rabinowitz for technical assistance. The research described herein was sponsored by the Defense Threat Reduction Agency (JSTO-CBD project number 44.10022-08-RD-B and TMTI project number 0048-09-RD-T ). The opinions, interpretation, conclusions and recommendations in this report are not necessarily endorsed by the U.S. Army.",

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AU - Patrick Reid, St

AU - Shurtleff, Amy C.

AU - Costantino, Julie A.

AU - Tritsch, Sarah R.

AU - Retterer, Cary

AU - Spurgers, Kevin B.

AU - Bavari, Sina

N1 - Funding Information: We thank Sean Van Tongeren for performing mouse infections and Keren Rabinowitz for technical assistance. The research described herein was sponsored by the Defense Threat Reduction Agency (JSTO-CBD project number 44.10022-08-RD-B and TMTI project number 0048-09-RD-T ). The opinions, interpretation, conclusions and recommendations in this report are not necessarily endorsed by the U.S. Army.

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AB - 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.

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