Heat shock protein-90-beta facilitates enterovirus 71 viral particles assembly

Abstract Molecular chaperones are reported to be crucial for virus propagation, but are not yet addressed in Human Enterovirus 71 (EV71). Here we describe the specific association of heat shock protein-90-beta (Hsp90β), but not alpha form (Hsp90α), with EV71 viral particles by the co-purification wi...

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Bibliographic Details
Published in:Virology (New York, N.Y.) N.Y.), 2013-09, Vol.443 (2), p.236-247
Main Authors: Wang, Robert Y.L, Kuo, Rei-Lin, Ma, Wei-Chieh, Huang, Hsing-I, Yu, Jau-Song, Yen, Sih-Min, Huang, Chi-Ruei, Shih, Shin-Ru
Format: Article
Language:English
Subjects:
60 APPLIED LIFE SCIENCES
Benzoquinones
Cell Line, Tumor
Centrifugation, Density Gradient
CULTURE MEDIA
ELECTRON MICROSCOPY
Enterovirus
Enterovirus 71
Enterovirus A, Human - genetics
Enterovirus A, Human - metabolism
Enterovirus A, Human - physiology
Enterovirus Infections - virology
Geldanamycin
Heat shock protein 90
HEAT-SHOCK PROTEINS
HSP90 Heat-Shock Proteins - genetics
HSP90 Heat-Shock Proteins - metabolism
Hsp90β
Human enterovirus 71
Humans
Immunohistochemistry
Infectious Disease
Lactams, Macrocyclic
PARTICLES
Proteins - genetics
Proteins - metabolism
Proteomics
PURIFICATION
RNA
RNA Interference
SACCHAROSE
ULTRACENTRIFUGATION
Viral particles assembly
Viral Proteins - genetics
Viral Proteins - metabolism
Virion - metabolism
Virus Assembly - drug effects
Virus Replication
VIRUSES
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Summary:Abstract Molecular chaperones are reported to be crucial for virus propagation, but are not yet addressed in Human Enterovirus 71 (EV71). Here we describe the specific association of heat shock protein-90-beta (Hsp90β), but not alpha form (Hsp90α), with EV71 viral particles by the co-purification with virions using sucrose density gradient ultracentrifugation, and by the colocalization with viral particles, as assessed by immunogold electron microscopy. The reduction of the Hsp90β protein using RNA interference decreased the correct assembly of viral particles, without affecting EV71 replication levels. Tracking ectopically expressed Hsp90β protein associated with EV71 virions revealed that Hsp90β protein was transmitted to new host cells through its direct association with infectious viral particles. Our findings suggest a new antiviral strategy in which extracellular Hsp90β protein is targeted to decrease the infectivity of EV71 and other enteroviruses, without affecting the broader functions of this constitutively expressed molecular chaperone.
ISSN:0042-6822
1096-0341
DOI:10.1016/j.virol.2013.05.001