The Host Heat Shock Protein MRJ/DNAJB6 Modulates Virus Infection
Journal
Frontiers in Microbiology
Journal Volume
10
Pages
2885
Date Issued
2019
Author(s)
Abstract
A variety of pathogens take advantage of cellular heat shock proteins (HSPs) to complete their life cycle and exert pathogenic effects. MRJ (DNAJB6), a member of the heat shock protein 40 family, acts as a molecular chaperone for a wide range of cellular processes. MRJ mutations are linked to human diseases, such as muscular dystrophy and neurodegenerative diseases. There are two MRJ isoforms generated by alternative use of terminal exons, which differ in their C-terminus. This mini-review summarizes how these two MRJ isoforms participate differentially in viral production and virulence, and the possibility for MRJ as a therapeutic target. ? Copyright ? 2019 Ko, Huang and Tarn.
Subjects
heat shock protein; Hsp40; morpholino oligonucleotide; MRJ; virus
SDGs
Other Subjects
chaperone; chaperonin 60; cyclin dependent kinase; cyclin dependent kinase 12; dynactin; glycogen synthase kinase 3beta; heat shock protein; heat shock protein 40; heat shock protein 70; heat shock protein 90; messenger RNA; nonstructural protein 3; nonstructural protein 5A; polymerase acidic protein; polymerase basic protein 1; polymerase basic protein 2; sequestosome 1; TAR DNA binding protein; unclassified drug; virus nucleoprotein; acquired immune deficiency syndrome; antiviral activity; cell adhesion; cell cycle regulation; dengue; Dengue virus; gene expression regulation; gene knockout; gene mutation; gene overexpression; heart ventricle hypertrophy; human; Human cytomegalovirus; Human immunodeficiency virus; Human respiratory syncytial virus; limb girdle muscular dystrophy; lipid metabolism; lower respiratory tract infection; nonhuman; nuclear localization signal; oligomerization; opportunistic infection; protein binding; protein expression; protein function; protein misfolding; protein targeting; Review; upregulation; virion; virogenesis; virus cell interaction; virus infection; virus replication; virus virulence
Publisher
Frontiers Media S.A.
Type
review