Chaperoning the : Current Knowledge and Future Directions

Overview

Journal Viruses

Publisher MDPI

Specialty Microbiology

Date 2018 Dec 15

PMID 30544818

Citations 7

Authors

Victor Latorre

Florian Mattenberger

Ron Geller

Affiliations

Soon will be listed here.

Abstract

The order harbors numerous viruses of significant relevance to human health, including both established and emerging infections. Currently, vaccines are only available for a small subset of these viruses, and antiviral therapies remain limited. Being obligate cellular parasites, viruses must utilize the cellular machinery for their replication and spread. Therefore, targeting cellular pathways used by viruses can provide novel therapeutic approaches. One of the key challenges confronted by both hosts and viruses alike is the successful folding and maturation of proteins. In cells, this task is faced by cellular molecular chaperones, a group of conserved and abundant proteins that oversee protein folding and help maintain protein homeostasis. In this review, we summarize the current knowledge of how the interact with cellular chaperones, highlight key gaps in our knowledge, and discuss the potential of chaperone inhibitors as antivirals.

Citing Articles

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References

Cantoni D, Rossman J . Ebolaviruses: New roles for old proteins. PLoS Negl Trop Dis. 2018; 12(5):e0006349. PMC: 5933699. DOI: 10.1371/journal.pntd.0006349. View

Hebert D, Molinari M . In and out of the ER: protein folding, quality control, degradation, and related human diseases. Physiol Rev. 2007; 87(4):1377-408. DOI: 10.1152/physrev.00050.2006. View

Ng D, Hiebert S, Lamb R . Different roles of individual N-linked oligosaccharide chains in folding, assembly, and transport of the simian virus 5 hemagglutinin-neuraminidase. Mol Cell Biol. 1990; 10(5):1989-2001. PMC: 360545. DOI: 10.1128/mcb.10.5.1989-2001.1990. View

Booth L, Roberts J, Ecroyd H, Tritsch S, Bavari S, Reid S . AR-12 Inhibits Multiple Chaperones Concomitant With Stimulating Autophagosome Formation Collectively Preventing Virus Replication. J Cell Physiol. 2016; 231(10):2286-302. PMC: 6327852. DOI: 10.1002/jcp.25431. View

Aragones L, Guix S, Ribes E, Bosch A, Pinto R . Fine-tuning translation kinetics selection as the driving force of codon usage bias in the hepatitis A virus capsid. PLoS Pathog. 2010; 6(3):e1000797. PMC: 2832697. DOI: 10.1371/journal.ppat.1000797. View

Ciechanover A, Kwon Y . Protein Quality Control by Molecular Chaperones in Neurodegeneration. Front Neurosci. 2017; 11:185. PMC: 5382173. DOI: 10.3389/fnins.2017.00185. View

Yam A, Xia Y, Lin H, Burlingame A, Gerstein M, Frydman J . Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies. Nat Struct Mol Biol. 2008; 15(12):1255-62. PMC: 2658641. DOI: 10.1038/nsmb.1515. View

Connor J, McKenzie M, Parks G, Lyles D . Antiviral activity and RNA polymerase degradation following Hsp90 inhibition in a range of negative strand viruses. Virology. 2007; 362(1):109-19. PMC: 1995422. DOI: 10.1016/j.virol.2006.12.026. View

Oliveira A, Simabuco F, Tamura R, Guerrero M, Ribeiro P, Libermann T . Human respiratory syncytial virus N, P and M protein interactions in HEK-293T cells. Virus Res. 2013; 177(1):108-12. DOI: 10.1016/j.virusres.2013.07.010. View

10.

Craig E . Hsp70 at the membrane: driving protein translocation. BMC Biol. 2018; 16(1):11. PMC: 5773037. DOI: 10.1186/s12915-017-0474-3. View

11.

Wang B, Wang Y, Frabutt D, Zhang X, Yao X, Hu D . Mechanistic understanding of -glycosylation in Ebola virus glycoprotein maturation and function. J Biol Chem. 2017; 292(14):5860-5870. PMC: 5392578. DOI: 10.1074/jbc.M116.768168. View

12.

Liljeroos L, Butcher S . Matrix proteins as centralized organizers of negative-sense RNA virions. Front Biosci (Landmark Ed). 2013; 18(2):696-715. DOI: 10.2741/4132. View

13.

Liang J, Sagum C, Bedford M, Sidhu S, Sudol M, Han Z . Chaperone-Mediated Autophagy Protein BAG3 Negatively Regulates Ebola and Marburg VP40-Mediated Egress. PLoS Pathog. 2017; 13(1):e1006132. PMC: 5226679. DOI: 10.1371/journal.ppat.1006132. View

14.

Munday D, Wu W, Smith N, Fix J, Noton S, Galloux M . Interactome analysis of the human respiratory syncytial virus RNA polymerase complex identifies protein chaperones as important cofactors that promote L-protein stability and RNA synthesis. J Virol. 2014; 89(2):917-30. PMC: 4300676. DOI: 10.1128/JVI.01783-14. View

15.

Wheeler D, Chase M, Senft A, Poynter S, Wong H, Page K . Extracellular Hsp72, an endogenous DAMP, is released by virally infected airway epithelial cells and activates neutrophils via Toll-like receptor (TLR)-4. Respir Res. 2009; 10:31. PMC: 2679007. DOI: 10.1186/1465-9921-10-31. View

16.

Roobol A, Sahyoun Z, Carden M . Selected subunits of the cytosolic chaperonin associate with microtubules assembled in vitro. J Biol Chem. 1999; 274(4):2408-15. DOI: 10.1074/jbc.274.4.2408. View

17.

Araki K, Nagata K . Protein folding and quality control in the ER. Cold Spring Harb Perspect Biol. 2012; 4(8):a015438. PMC: 3405861. DOI: 10.1101/cshperspect.a015438. View

18.

Chang J, Warren T, Zhao X, Gill T, Guo F, Wang L . Small molecule inhibitors of ER α-glucosidases are active against multiple hemorrhagic fever viruses. Antiviral Res. 2013; 98(3):432-40. PMC: 3663898. DOI: 10.1016/j.antiviral.2013.03.023. View

19.

Wang Y, Jin F, Wang R, Li F, Wu Y, Kitazato K . HSP90: a promising broad-spectrum antiviral drug target. Arch Virol. 2017; 162(11):3269-3282. DOI: 10.1007/s00705-017-3511-1. View

20.

Brehme M, Voisine C, Rolland T, Wachi S, Soper J, Zhu Y . A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease. Cell Rep. 2014; 9(3):1135-50. PMC: 4255334. DOI: 10.1016/j.celrep.2014.09.042. View