title: Broad action of Hsp90 as a host chaperone required for viral replication.
abstract: Viruses are intracellular pathogens responsible for a vast number of human diseases. Due to their small genome size, viruses rely primarily on the biosynthetic apparatus of the host for their replication. Recent work has shown that the molecular chaperone Hsp90 is nearly universally required for viral protein homeostasis. As observed for many endogenous cellular proteins, numerous different viral proteins have been shown to require Hsp90 for their folding, assembly, and maturation. Importantly, the unique characteristics of viral replication cause viruses to be hypersensitive to Hsp90 inhibition, thus providing a novel therapeutic avenue for the development of broad-spectrum antiviral drugs. The major developments in this emerging field are hereby discussed. This article is part of a Special Issue entitled: Heat Shock Protein 90 (HSP90).
authors.affiliation: Department of Biology and BioX Program, Stanford University, Stanford, CA, USA.
authors.forename: Ron
authors.initials: R
authors.lastname: Geller
authors.forename: Shuhei
authors.initials: S
authors.lastname: Taguwa
authors.forename: Judith
authors.initials: J
authors.lastname: Frydman
mesh_terms: D000998:Antiviral Agents / Q000737:chemistry; D018841:HSP90 Heat-Shock Proteins / Q000502:physiology*; D006801:Humans; D018832:Molecular Chaperones / Q000502:physiology*; D014779:Virus Replication / Q000187:drug effects / Q000502:physiology*
chemical_list: D000998:Antiviral Agents; D018841:HSP90 Heat-Shock Proteins; D018832:Molecular Chaperones