Hsp90 is involved in pseudorabies virus virion assembly via stabilizing major capsid protein VP5.

Abstract:

:Many viruses utilize molecular chaperone heat shock protein 90 (Hsp90) for protein folding and stabilization, however, the role of Hsp90 in herpesvirus lifecycle is obscure. Here, we provide evidence that Hsp90 participates in pseudorabies virus (PRV) replication. Viral growth kinetics assays show that Hsp90 inhibitor geldanamycin (GA) abrogates PRV replication at the post-penetration step. Transmission electron microscopy demonstrates that dysfunction of Hsp90 diminishes the quantity of PRV nucleocapsids. Overexpression and knockdown of Hsp90 suggest that de novo Hsp90 is involved in PRV replication. Mechanismly, dysfunction of Hsp90 inhibits PRV major capsid protein VP5 expression. Co-immunoprecipitation and indirect immunofluorescence assays indicate that Hsp90 interacts with VP5. Interestingly, Hsp70, a collaborator of Hsp90, also interacts with VP5, but doesn't affect PRV growth. Finally, inhibition of Hsp90 results in PRV VP5 degradation in a proteasome-dependent manner. Collectively, our data suggest that Hsp90 contributes to PRV virion assembly and replication via stabilization of VP5.

journal_name

Virology

journal_title

Virology

authors

Zhang WJ,Wang RQ,Li LT,Fu W,Chen HC,Liu ZF

doi

10.1016/j.virol.2020.10.013

subject

Has Abstract

pub_date

2021-01-15 00:00:00

pages

70-80

eissn

0042-6822

issn

1096-0341

pii

S0042-6822(20)30222-1

journal_volume

553

pub_type

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