Broad action of Hsp90 as a host chaperone required for viral replication.
Biochim Biophys Acta
; 1823(3): 698-706, 2012 Mar.
Article
de En
| MEDLINE
| ID: mdl-22154817
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).
Texte intégral:
1
Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Réplication virale
/
Chaperons moléculaires
/
Protéines du choc thermique HSP90
Limites:
Humans
Langue:
En
Journal:
Biochim Biophys Acta
Année:
2012
Type de document:
Article
Pays d'affiliation:
États-Unis d'Amérique