Heat Shock Protein 90 Ensures the Integrity of Rubella Virus p150 Protein and Supports Viral Replication

Author:

Sakata Masafumi1,Katoh Hiroshi1,Otsuki Noriyuki1,Okamoto Kiyoko1,Nakatsu Yuichiro1,Lim Chang-Kweng2,Saijo Masayuki2ORCID,Takeda Makoto1ORCID,Mori Yoshio1

Affiliation:

1. Department of Virology 3, National Institute of Infectious Diseases, Tokyo, Japan

2. Department of Virology 1, National Institute of Infectious Diseases, Tokyo, Japan

Abstract

Accumulating evidence indicates that RNA viruses use numerous host factors during replication of their genomes. However, the host factors involved in rubella virus (RUBV) genome replication are largely unknown. In this study, we demonstrate that the HSP90 molecular chaperone is needed for the efficient replication of the RUBV genome. Further, we reveal that HSP90 interacts with RUBV nonstructural protein p150 and its precursor polyprotein, p200. HSP90 contributes to the stability of p150 and the processing of p200 via its protease domain in the p150 region. We conclude that the cellular molecular chaperone HSP90 is a key host factor for functional maturation of nonstructural proteins for RUBV genome replication. These findings provide novel insight into this host-virus interaction.

Funder

Takeda Science Foundation

MEXT | Japan Society for the Promotion of Science

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

Reference72 articles.

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