{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T09:22:24Z","timestamp":1790846544786,"version":"4.1.0"},"reference-count":122,"publisher":"MDPI AG","issue":"12","license":[{"start":{"date-parts":[[2018,12,8]],"date-time":"2018-12-08T00:00:00Z","timestamp":1544227200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100011596","name":"Conselleria d'Educaci\u00f3, Investigaci\u00f3, Cultura i Esport","doi-asserted-by":"publisher","award":["SEJI\/2017\/006"],"award-info":[{"award-number":["SEJI\/2017\/006"]}],"id":[{"id":"10.13039\/501100011596","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001704","name":"European Society of Clinical Microbiology and Infectious Diseases","doi-asserted-by":"publisher","award":["Research Grant 2017"],"award-info":[{"award-number":["Research Grant 2017"]}],"id":[{"id":"10.13039\/501100001704","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100014440","name":"Ministerio de Ciencia, Innovaci\u00f3n y Universidades","doi-asserted-by":"publisher","award":["BES-2016-076677"],"award-info":[{"award-number":["BES-2016-076677"]}],"id":[{"id":"10.13039\/100014440","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003329","name":"Ministerio de Econom\u00eda y Competitividad","doi-asserted-by":"publisher","award":["RYC-2015-17517"],"award-info":[{"award-number":["RYC-2015-17517"]}],"id":[{"id":"10.13039\/501100003329","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Viruses"],"abstract":"<jats:p>The order Mononegavirales 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 Mononegavirales interact with cellular chaperones, highlight key gaps in our knowledge, and discuss the potential of chaperone inhibitors as antivirals.<\/jats:p>","DOI":"10.3390\/v10120699","type":"journal-article","created":{"date-parts":[[2018,12,10]],"date-time":"2018-12-10T03:36:41Z","timestamp":1544413001000},"page":"699","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["Chaperoning the Mononegavirales: Current Knowledge and Future Directions"],"prefix":"10.3390","volume":"10","author":[{"given":"Victor","family":"Latorre","sequence":"first","affiliation":[{"name":"Institute for Integrative Systems Biology (I2SysBio), Universitat de Valencia-CSIC, 46980 Valencia, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2727-0284","authenticated-orcid":false,"given":"Florian","family":"Mattenberger","sequence":"additional","affiliation":[{"name":"Institute for Integrative Systems Biology (I2SysBio), Universitat de Valencia-CSIC, 46980 Valencia, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7612-4611","authenticated-orcid":false,"given":"Ron","family":"Geller","sequence":"additional","affiliation":[{"name":"Institute for Integrative Systems Biology (I2SysBio), Universitat de Valencia-CSIC, 46980 Valencia, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2018,12,8]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"2283","DOI":"10.1007\/s00705-018-3814-x","article-title":"Taxonomy of the order Mononegavirales: Update 2018","volume":"163","author":"Amarasinghe","year":"2018","journal-title":"Arch. Virol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/bs.aivir.2016.12.001","article-title":"Zoonotic Potential of Emerging Paramyxoviruses: Knowns and Unknowns","volume":"98","author":"Thibault","year":"2017","journal-title":"Adv. Virus Res."},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Coltart, C.E.M., Lindsey, B., Ghinai, I., Johnson, A.M., and Heymann, D.L. (2017). The Ebola outbreak, 2013-2016: Old lessons for new epidemics. Phil. Trans. R. Soc. Lond. B Biol. Sci., 372.","DOI":"10.1098\/rstb.2016.0297"},{"key":"ref_4","first-page":"61","article-title":"Transcription and replication of nonsegmented negative-strand RNA viruses","volume":"283","author":"Whelan","year":"2004","journal-title":"Curr. Top. Microbiol. Immunol."},{"key":"ref_5","unstructured":"Knipe, D.M., and Howley, P.M. (2013). Mononegavirales. Fields Virology, Wolters Kluwer Health\/Lippincott Williams & Wilkins."},{"key":"ref_6","first-page":"103","article-title":"Nucleocapsid structure and function","volume":"329","author":"Longhi","year":"2009","journal-title":"Curr. Top. Microbiol. Immunol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.coviro.2013.03.008","article-title":"The polymerase of negative-stranded RNA viruses","volume":"3","author":"Morin","year":"2013","journal-title":"Curr. Opin. Virol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"3091","DOI":"10.1007\/s00018-017-2556-3","article-title":"How order and disorder within paramyxoviral nucleoproteins and phosphoproteins orchestrate the molecular interplay of transcription and replication","volume":"74","author":"Longhi","year":"2017","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"696","DOI":"10.2741\/4132","article-title":"Matrix proteins as centralized organizers of negative-sense RNA virions","volume":"18","author":"Liljeroos","year":"2013","journal-title":"Front. Biosci."},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Cantoni, D., and Rossman, J.S. (2018). Ebolaviruses: New roles for old proteins. PLoS Negl. Trop. Dis., 12.","DOI":"10.1371\/journal.pntd.0006349"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"M110","DOI":"10.1074\/mcp.M110.007443","article-title":"Proteomic analysis of virus-host interactions in an infectious context using recombinant viruses","volume":"10","author":"Komarova","year":"2011","journal-title":"Mol. Cell. Proteom."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1186\/s13073-014-0115-1","article-title":"Virus-host interactomics: New insights and opportunities for antiviral drug discovery","volume":"6","author":"Vonderscher","year":"2014","journal-title":"Genome Med."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1430","DOI":"10.1126\/science.aaf1084","article-title":"Translation dynamics of single mRNAs in live cells and neurons","volume":"352","author":"Wu","year":"2016","journal-title":"Science"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1016\/S0968-0004(01)01938-7","article-title":"Macromolecular crowding: Obvious but underappreciated","volume":"26","author":"Ellis","year":"2001","journal-title":"Trends Biochem. Sci."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"aac4354","DOI":"10.1126\/science.aac4354","article-title":"In vivo aspects of protein folding and quality control","volume":"353","author":"Balchin","year":"2016","journal-title":"Science"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1038\/nature10098","article-title":"Global quantification of mammalian gene expression control","volume":"473","author":"Busse","year":"2011","journal-title":"Nature"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.1016\/j.celrep.2014.09.042","article-title":"A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease","volume":"9","author":"Brehme","year":"2014","journal-title":"Cell Rep."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1007\/s12192-013-0413-3","article-title":"Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis","volume":"18","author":"Finka","year":"2013","journal-title":"Cell Stress Chaperones"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/j.tibs.2008.10.009","article-title":"Do viral proteins possess unique biophysical features?","volume":"34","author":"Tokuriki","year":"2009","journal-title":"Trends Biochem. Sci."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"4433","DOI":"10.1007\/s00018-016-2299-6","article-title":"Mechanisms of viral mutation","volume":"73","author":"Sanjuan","year":"2016","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"596","DOI":"10.1016\/j.sbi.2009.08.003","article-title":"Stability effects of mutations and protein evolvability","volume":"19","author":"Tokuriki","year":"2009","journal-title":"Curr. Opin. Struct. Biol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1146\/annurev-biochem-060208-092442","article-title":"Molecular chaperone functions in protein folding and proteostasis","volume":"82","author":"Kim","year":"2013","journal-title":"Annu. Rev. Biochem."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"185","DOI":"10.3389\/fnins.2017.00185","article-title":"Protein quality control by molecular chaperones in neurodegeneration","volume":"11","author":"Ciechanover","year":"2017","journal-title":"Front. Neurosci."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1016\/j.molcel.2018.01.004","article-title":"Cellular Handling of Protein Aggregates by Disaggregation Machines","volume":"69","author":"Mogk","year":"2018","journal-title":"Mol. Cell"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1016\/j.molcel.2017.05.031","article-title":"The UPRER: Sensor and Coordinator of Organismal Homeostasis","volume":"66","author":"Frakes","year":"2017","journal-title":"Mol. Cell"},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Chatterjee, S., and Burns, T.F. (2017). Targeting heat shock proteins in cancer: A promising therapeutic approach. Int. J. Mol. Sci., 18.","DOI":"10.3390\/ijms18091978"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1","DOI":"10.9734\/BJMMR\/2016\/24631","article-title":"The Hsp90 Chaperone Machinery: An Important Hub in Protein Interaction Networks","volume":"14","author":"Radons","year":"2016","journal-title":"Br. J. Med. Med. Res."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1007\/s12192-016-0676-6","article-title":"The human HSP70 family of chaperones: Where do we stand?","volume":"21","author":"Radons","year":"2016","journal-title":"Cell Stress Chaperones"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"670","DOI":"10.1007\/s00018-004-4464-6","article-title":"Hsp70 chaperones: Cellular functions and molecular mechanism","volume":"62","author":"Mayer","year":"2005","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"26","DOI":"10.3389\/fmolb.2015.00026","article-title":"The role of molecular chaperones in clathrin mediated vesicular trafficking","volume":"2","author":"Sousa","year":"2015","journal-title":"Front. Mol. Biosci."},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"Craig, E.A. (2018). Hsp70 at the membrane: Driving protein translocation. BMC Biol., 16.","DOI":"10.1186\/s12915-017-0474-3"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1575","DOI":"10.1016\/j.jmb.2015.02.004","article-title":"How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions","volume":"427","author":"Clerico","year":"2015","journal-title":"J. Mol. Biol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1038\/nrm2941","article-title":"The HSP70 chaperone machinery: J proteins as drivers of functional specificity","volume":"11","author":"Kampinga","year":"2010","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/978-3-319-11731-7_1","article-title":"GrpE, Hsp110\/Grp170, HspBP1\/Sil1 and BAG domain proteins: Nucleotide exchange factors for Hsp70 molecular chaperones","volume":"78","author":"Bracher","year":"2015","journal-title":"Subcell. Biochem."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1007\/s12192-010-0248-0","article-title":"Versatile TPR domains accommodate different modes of target protein recognition and function","volume":"16","author":"Allan","year":"2011","journal-title":"Cell Stress Chaperones"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"177","DOI":"10.3389\/fnmol.2017.00177","article-title":"The Role of the Multifunctional BAG3 Protein in Cellular Protein Quality Control and in Disease","volume":"10","author":"Behl","year":"2017","journal-title":"Front. Mol. Neurosci."},{"key":"ref_37","doi-asserted-by":"crossref","unstructured":"Tanguay, R.M., and Hightower, L.E. (2015). The Multicolored World of the Human HSPB Family. The Big Book on Small Heat Shock Proteins, Springer International Publishing.","DOI":"10.1007\/978-3-319-16077-1"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"1537","DOI":"10.1016\/j.jmb.2015.02.002","article-title":"A first line of stress defense: Small heat shock proteins and their function in protein homeostasis","volume":"427","author":"Haslbeck","year":"2015","journal-title":"J. Mol. Biol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1038\/nrm.2017.20","article-title":"The HSP90 chaperone machinery","volume":"18","author":"Schopf","year":"2017","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1016\/j.molcel.2018.03.028","article-title":"Hsp90 Breaks the Deadlock of the Hsp70 Chaperone System","volume":"70","author":"Kityk","year":"2018","journal-title":"Mol. Cell"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"3269","DOI":"10.1007\/s00705-017-3511-1","article-title":"HSP90: A promising broad-spectrum antiviral drug target","volume":"162","author":"Wang","year":"2017","journal-title":"Arch. Virol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"698","DOI":"10.1016\/j.bbamcr.2011.11.007","article-title":"Broad action of Hsp90 as a host chaperone required for viral replication","volume":"1823","author":"Geller","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Calderwood, S.K., and Prince, T.L. (2018). Clinical Evaluation and Biomarker Profiling of Hsp90 Inhibitors. Chaperones: Methods and Protocols, Springer.","DOI":"10.1007\/978-1-4939-7477-1"},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Aragon\u00e8s, L., Guix, S., Ribes, E., Bosch, A., and Pint\u00f3, R.M. (2010). Fine-tuning translation kinetics selection as the driving force of codon usage bias in the hepatitis A virus capsid. PLoS Pathog., 6.","DOI":"10.1371\/journal.ppat.1000797"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"2919","DOI":"10.1016\/j.jmb.2015.04.013","article-title":"The Mechanism and Function of Group II Chaperonins","volume":"427","author":"Lopez","year":"2015","journal-title":"J. Mol. Biol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1255","DOI":"10.1038\/nsmb.1515","article-title":"Defining the TRiC\/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies","volume":"15","author":"Yam","year":"2008","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"1377","DOI":"10.1152\/physrev.00050.2006","article-title":"In and out of the ER: Protein folding, quality control, degradation, and related human diseases","volume":"87","author":"Hebert","year":"2007","journal-title":"Physiol. Rev."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1016\/j.ceb.2010.05.005","article-title":"Quality and quantity control at the endoplasmic reticulum","volume":"22","author":"Hegde","year":"2010","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"a015438","DOI":"10.1101\/cshperspect.a015438","article-title":"SUP: Protein folding and quality control in the ER","volume":"4","author":"Araki","year":"2012","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"710","DOI":"10.1074\/mcp.M111.016550","article-title":"An Interaction Map of Endoplasmic Reticulum Chaperones and Foldases","volume":"11","author":"Jansen","year":"2012","journal-title":"Mol. Cell. Proteom."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"3188","DOI":"10.1128\/JVI.03343-14","article-title":"Heat shock protein 70 regulates degradation of the mumps virus phosphoprotein via the ubiquitin-proteasome pathway","volume":"89","author":"Katoh","year":"2015","journal-title":"J. Virol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"43822","DOI":"10.18632\/oncotarget.16517","article-title":"Rabies viruses leader RNA interacts with host Hsc70 and inhibits virus replication","volume":"8","author":"Zhang","year":"2017","journal-title":"Oncotarget"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"4743","DOI":"10.1128\/JVI.06501-11","article-title":"Hsp70 Protein Positively Regulates Rabies Virus Infection","volume":"86","author":"Lahaye","year":"2012","journal-title":"J. Virol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1186\/1465-9921-10-31","article-title":"Extracellular Hsp72, an endogenous DAMP, is released by virally infected airway epithelial cells and activates neutrophils via Toll-like receptor (TLR)-4","volume":"10","author":"Wheeler","year":"2009","journal-title":"Respir. Res."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1159\/000449101","article-title":"Human Metapneumovirus Impairs Apoptosis of Nasal Epithelial Cells in Asthma via HSP70","volume":"9","author":"Baturcam","year":"2017","journal-title":"J. Innate Immun."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1016\/j.virusres.2013.07.010","article-title":"Human respiratory syncytial virus N, P and M protein interactions in HEK-293T cells","volume":"177","author":"Oliveira","year":"2013","journal-title":"Virus Res."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"646","DOI":"10.3390\/cells1030646","article-title":"Virus-heat shock protein interaction and a novel axis for innate antiviral immunity","volume":"1","author":"Kim","year":"2012","journal-title":"Cells"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s10254-004-0025-5","article-title":"Recruitment of Hsp70 chaperones: A crucial part of viral survival strategies","volume":"Volume 153","author":"Mayer","year":"2005","journal-title":"Reviews of Physiology, Biochemistry and Pharmacology"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1128\/jvi.44.2.703-707.1982","article-title":"Newcastle disease virus stimulates the cellular accumulation of stress (heat shock) mRNAs and proteins","volume":"44","author":"Collins","year":"1982","journal-title":"J. Virol."},{"key":"ref_60","first-page":"109","article-title":"Cellular stress response induces selective intranuclear trafficking and accumulation of morbillivirus major core protein","volume":"68","author":"Oglesbee","year":"1993","journal-title":"Lab. Investig."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/j.virol.2005.05.004","article-title":"Evidence for an association between heat shock protein 70 and the respiratory syncytial virus polymerase complex within lipid-raft membranes during virus infection","volume":"338","author":"Brown","year":"2005","journal-title":"Virology"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"1829","DOI":"10.1074\/mcp.M110.001651","article-title":"Protein analysis of purified respiratory syncytial virus particles reveals an important role for heat shock protein 90 in virus particle assembly","volume":"9","author":"Radhakrishnan","year":"2010","journal-title":"Mol. Cell. Proteom."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"7948","DOI":"10.1128\/JVI.00554-09","article-title":"Functional Characterization of Negri Bodies (NBs) in Rabies Virus-Infected Cells: Evidence that NBs Are Sites of Viral Transcription and Replication","volume":"83","author":"Lahaye","year":"2009","journal-title":"J. Virol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"556","DOI":"10.1006\/viro.1993.1072","article-title":"Enhanced production of morbillivirus gene-specific RNAs following induction of the cellular stress response in stable persistent infection","volume":"192","author":"Oglesbee","year":"1993","journal-title":"Virology"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"2125","DOI":"10.1099\/0022-1317-77-9-2125","article-title":"The Highly Inducible Member of the 70 kDa Family of Heat Shock Proteins Increases Canine Distemper Virus Polymerase Activity","volume":"77","author":"Oglesbee","year":"1996","journal-title":"J. Gen. Virol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1769","DOI":"10.1099\/0022-1317-79-7-1769","article-title":"The cellular stress response increases measles virus-induced cytopathic effect","volume":"79 Pt 7","author":"Vasconcelos","year":"1998","journal-title":"J. Gen. Virol."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"3560","DOI":"10.1128\/JVI.73.5.3560-3566.1999","article-title":"Enhanced measles virus cDNA rescue and gene expression after heat shock","volume":"73","author":"Parks","year":"1999","journal-title":"J. Virol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/S0166-3542(98)00017-5","article-title":"Interferon-alpha inhibits the emergence of cellular stress response-dependent morbillivirus large plaque variants","volume":"38","author":"Heller","year":"1998","journal-title":"Antivir. Res."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"2239","DOI":"10.1099\/0022-1317-79-9-2239","article-title":"Constitutive overexpression of the major inducible 70 kDa heat shock protein mediates large plaque formation by measles virus","volume":"79 Pt 9","author":"Vasconcelos","year":"1998","journal-title":"J. Gen. Virol."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"8737","DOI":"10.1128\/JVI.76.17.8737-8746.2002","article-title":"Identification and characterization of a regulatory domain on the carboxyl terminus of the measles virus nucleocapsid protein","volume":"76","author":"Zhang","year":"2002","journal-title":"J. Virol."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"11031","DOI":"10.1128\/JVI.01438-06","article-title":"hsp72, a host determinant of measles virus neurovirulence","volume":"80","author":"Carsillo","year":"2006","journal-title":"J. Virol."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"10668","DOI":"10.1128\/JVI.00872-13","article-title":"hsp70-Dependent Antiviral Immunity against Cytopathic Neuronal Infection by Vesicular Stomatitis Virus","volume":"87","author":"Kim","year":"2013","journal-title":"J. Virol."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/j.virol.2005.03.035","article-title":"Hsp72 recognizes a P binding motif in the measles virus N protein C-terminus","volume":"337","author":"Zhang","year":"2005","journal-title":"Virology"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1002\/jmr.982","article-title":"High affinity binding between Hsp70 and the C-terminal domain of the measles virus nucleoprotein requires an Hsp40 co-chaperone","volume":"23","author":"Couturier","year":"2010","journal-title":"J. Mol. Recognit."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"2904","DOI":"10.1128\/JVI.80.6.2904-2912.2006","article-title":"A single codon in the nucleocapsid protein C terminus contributes to in vitro and in vivo fitness of Edmonston measles virus","volume":"80","author":"Carsillo","year":"2006","journal-title":"J. Virol."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"4290","DOI":"10.1021\/acs.jproteome.6b00337","article-title":"Elucidation of the Cellular Interactome of Ebola Virus Nucleoprotein and Identification of Therapeutic Targets","volume":"15","author":"Wu","year":"2016","journal-title":"J. Proteome Res."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.antiviral.2017.08.005","article-title":"An RNA polymerase II-driven Ebola virus minigenome system as an advanced tool for antiviral drug screening","volume":"146","author":"Nelson","year":"2017","journal-title":"Antivir. Res."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"3970","DOI":"10.1038\/s41598-018-22328-3","article-title":"Recombinant RNA-Dependent RNA Polymerase Complex of Ebola Virus","volume":"8","author":"Tchesnokov","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"917","DOI":"10.1128\/JVI.01783-14","article-title":"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","volume":"89","author":"Munday","year":"2015","journal-title":"J. Virol."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"e02220-16","DOI":"10.1128\/JVI.02220-16","article-title":"Heat Shock Protein 90 Ensures Efficient Mumps Virus Replication by Assisting with Viral Polymerase Complex Formation","volume":"91","author":"Katoh","year":"2017","journal-title":"J. Virol."},{"key":"ref_81","first-page":"9831","article-title":"A small stem-loop structure of the Ebola virus trailer is essential for replication and interacts with heat-shock protein A8","volume":"44","author":"Diaz","year":"2016","journal-title":"Nucleic Acids Res."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"7777","DOI":"10.1128\/JVI.00460-12","article-title":"The interactome of the human respiratory syncytial virus NS1 protein highlights multiple effects on host cell biology","volume":"86","author":"Wu","year":"2012","journal-title":"J. Virol."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"2690","DOI":"10.1074\/mcp.M110.003418","article-title":"Identification of essential filovirion-associated host factors by serial proteomic analysis and RNAi screen","volume":"9","author":"Spurgers","year":"2010","journal-title":"Mol. Cell. Proteom."},{"key":"ref_84","doi-asserted-by":"crossref","unstructured":"Liang, J., Sagum, C.A., Bedford, M.T., Sidhu, S.S., Sudol, M., Han, Z., and Harty, R.N. (2017). Chaperone-Mediated Autophagy Protein BAG3 Negatively Regulates Ebola and Marburg VP40-Mediated Egress. PLoS Pathog., 13.","DOI":"10.1371\/journal.ppat.1006519"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1016\/j.cell.2015.06.018","article-title":"Structure of the L Protein of Vesicular Stomatitis Virus from Electron Cryomicroscopy","volume":"162","author":"Liang","year":"2015","journal-title":"Cell"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"6642","DOI":"10.1128\/JVI.00602-16","article-title":"HSP90 Chaperoning in Addition to Phosphoprotein Required for Folding but Not for Supporting Enzymatic Activities of Measles and Nipah Virus L Polymerases","volume":"90","author":"Bloyet","year":"2016","journal-title":"J. Virol."},{"key":"ref_87","doi-asserted-by":"crossref","unstructured":"Geller, R., Andino, R., and Frydman, J. (2013). Hsp90 inhibitors exhibit resistance-free antiviral activity against respiratory syncytial virus. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0056762"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.virol.2006.12.026","article-title":"Antiviral activity and RNA polymerase degradation following Hsp90 inhibition in a range of negative strand viruses","volume":"362","author":"Connor","year":"2007","journal-title":"Virology"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"27123","DOI":"10.1038\/srep27123","article-title":"The co-chaperone Cdc37 regulates the rabies virus phosphoprotein stability by targeting to Hsp90AA1 machinery","volume":"6","author":"Xu","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"7608","DOI":"10.1128\/JVI.03186-12","article-title":"Cellular Chaperonin CCT Contributes to Rabies Virus Replication during Infection","volume":"87","author":"Zhang","year":"2013","journal-title":"J. Virol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"590","DOI":"10.1111\/1348-0421.12186","article-title":"The chaperonin CCT\u03b1 is required for efficient transcription and replication of rabies virus","volume":"58","author":"Zhang","year":"2014","journal-title":"Microbiol. Immunol."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"2408","DOI":"10.1074\/jbc.274.4.2408","article-title":"Selected subunits of the cytosolic chaperonin associate with microtubules assembled in vitro","volume":"274","author":"Roobol","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"5120","DOI":"10.1021\/pr500556d","article-title":"Elucidation of the Ebola virus VP24 cellular interactome and disruption of virus biology through targeted inhibition of host-cell protein function","volume":"13","author":"Wu","year":"2014","journal-title":"J. Proteome Res."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/0042-6822(90)90196-X","article-title":"Selective and transient association of Sendai virus HN glycoprotein with BiP","volume":"175","author":"Roux","year":"1990","journal-title":"Virology"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"3590","DOI":"10.1128\/jvi.65.7.3590-3597.1991","article-title":"A Flux of the paramyxovirus hemagglutinin-neuraminidase glycoprotein through the endoplasmic reticulum activates transcription of the GRP78-BiP gene","volume":"65","author":"Watowich","year":"1991","journal-title":"J. Virol."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1002\/1097-4644(20010301)80:3<441::AID-JCB170>3.0.CO;2-C","article-title":"An endoplasmic reticulum-specific stress-activated caspase (caspase-12) is implicated in the apoptosis of A549 epithelial cells by respiratory syncytial virus","volume":"80","author":"Bitko","year":"2001","journal-title":"J. Cell. Biochem."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"2055","DOI":"10.1007\/s007050170020","article-title":"The measles virus (MV) glycoproteins interact with cellular chaperones in the endoplasmic reticulum and MV infection upregulates chaperone expression","volume":"146","author":"Bolt","year":"2001","journal-title":"Arch. Virol."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/j.antiviral.2014.07.004","article-title":"HSPA5 is an essential host factor for Ebola virus infection","volume":"109","author":"Shurtleff","year":"2014","journal-title":"Antivir. Res."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"3273","DOI":"10.1083\/jcb.109.6.3273","article-title":"Intracellular maturation and transport of the SV5 type II glycoprotein hemagglutinin-neuraminidase: Specific and transient association with GRP78-BiP in the endoplasmic reticulum and extensive internalization from the cell surface","volume":"109","author":"Ng","year":"1989","journal-title":"J. Cell Biol."},{"key":"ref_100","first-page":"1989","article-title":"Different roles of individual N-linked oligosaccharide chains in folding, assembly, and transport of the simian virus 5 hemagglutinin-neuraminidase","volume":"10","author":"Ng","year":"1990","journal-title":"Mol. Cell. Biol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"1177","DOI":"10.1099\/0022-1317-73-5-1177","article-title":"Intracellular processing of the human respiratory syncytial virus fusion glycoprotein: Amino acid substitutions affecting folding, transport and cleavage","volume":"73","author":"Anderson","year":"1992","journal-title":"J. Gen. Virol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"3742","DOI":"10.1128\/jvi.71.5.3742-3750.1997","article-title":"Folding of rabies virus glycoprotein: Epitope acquisition and interaction with endoplasmic reticulum chaperones","volume":"71","author":"Gaudin","year":"1997","journal-title":"J. Virol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"2286","DOI":"10.1002\/jcp.25431","article-title":"AR-12 Inhibits Multiple Chaperones Concomitant With Stimulating Autophagosome Formation Collectively Preventing Virus Replication","volume":"231","author":"Booth","year":"2016","journal-title":"J. Cell. Physiol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"2552","DOI":"10.1002\/jcp.25014","article-title":"GRP78\/Dna K Is a Target for Nexavar\/Stivarga\/Votrient in the Treatment of Human Malignancies, Viral Infections and Bacterial Diseases","volume":"230","author":"Roberts","year":"2015","journal-title":"J. Cell. Physiol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"1661","DOI":"10.1002\/jcp.24919","article-title":"GRP78\/BiP\/HSPA5\/Dna K is a universal therapeutic target for human disease","volume":"230","author":"Booth","year":"2015","journal-title":"J. Cell. Physiol."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"5860","DOI":"10.1074\/jbc.M116.768168","article-title":"Mechanistic understanding of N-glycosylation in Ebola virus glycoprotein maturation and function","volume":"292","author":"Wang","year":"2017","journal-title":"J. Biol. Chem."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1126\/science.7939687","article-title":"Folding of VSV G protein: Sequential interaction with BiP and calnexin","volume":"266","author":"Hammond","year":"1994","journal-title":"Science"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"1173","DOI":"10.1091\/mbc.6.9.1173","article-title":"Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins","volume":"6","author":"Peterson","year":"1995","journal-title":"Mol. Biol. Cell"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"6970","DOI":"10.1073\/pnas.0908536107","article-title":"Endoplasmic reticulum chaperone gp96 is essential for infection with vesicular stomatitis virus","volume":"107","author":"Bloor","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/j.antiviral.2010.04.015","article-title":"Inhibition of heat-shock protein 90 reduces Ebola virus replication","volume":"87","author":"Smith","year":"2010","journal-title":"Antivir. Res."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"1024","DOI":"10.1038\/gt.2008.30","article-title":"Heat shock protein inhibitors increase the efficacy of measles virotherapy","volume":"15","author":"Liu","year":"2008","journal-title":"Gene Ther."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1111\/jphp.12349","article-title":"Proteomic analysis of mitochondria in respiratory epithelial cells infected with human respiratory syncytial virus and functional implications for virus and cell biology","volume":"67","author":"Munday","year":"2015","journal-title":"J. Pharm. Pharmacol."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1101\/gad.1505307","article-title":"Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance","volume":"21","author":"Geller","year":"2007","journal-title":"Genes Dev."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"305","DOI":"10.2334\/josnusd.57.305","article-title":"Effect of ionomycin on interaction of calnexin with vesicular stomatitis virus glycoprotein is cell type-specific","volume":"57","author":"Okudera","year":"2015","journal-title":"J. Oral Sci."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1016\/j.antiviral.2013.03.023","article-title":"Small molecule inhibitors of ER \u03b1-glucosidases are active against multiple hemorrhagic fever viruses","volume":"98","author":"Chang","year":"2013","journal-title":"Antivir. Res."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1111\/j.1476-5381.2010.01064.x","article-title":"The endoplasmic reticulum protein folding factory and its chaperones: New targets for drug discovery?","volume":"162","author":"McLaughlin","year":"2011","journal-title":"Br. J. Pharmacol."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"998","DOI":"10.1128\/JVI.02710-12","article-title":"hsp70 and a novel axis of type I interferon-dependent antiviral immunity in the measles virus-infected brain","volume":"87","author":"Kim","year":"2013","journal-title":"J. Virol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/j.brainres.2003.12.041","article-title":"Hyperthermic pre-conditioning promotes measles virus clearance from brain in a mouse model of persistent infection","volume":"1004","author":"Carsillo","year":"2004","journal-title":"Brain Res."},{"key":"ref_119","doi-asserted-by":"crossref","unstructured":"Pockley, A.G., and Henderson, B. (2018). Extracellular cell stress (heat shock) proteins-immune responses and disease: An overview. Philos. Trans. R. Soc. Lond. B Biol. Sci., 373.","DOI":"10.1098\/rstb.2016.0522"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"4320","DOI":"10.1002\/pmic.201000228","article-title":"Quantitative proteomic analysis of A549 cells infected with human respiratory syncytial virus subgroup B using SILAC coupled to LC-MS\/MS","volume":"10","author":"Munday","year":"2010","journal-title":"Proteom."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"1108","DOI":"10.1016\/j.cell.2015.10.046","article-title":"Defining Hsp70 Subnetworks in Dengue Virus Replication Reveals Key Vulnerability in Flavivirus Infection","volume":"163","author":"Taguwa","year":"2015","journal-title":"Cell"},{"key":"ref_122","doi-asserted-by":"crossref","unstructured":"Joshi, S., Wang, T., Araujo, T.L.S., Sharma, S., Brodsky, J.L., and Chiosis, G. (2018). Adapting to stress\u2014Chaperome networks in cancer. Nat. Rev. Cancer, 1\u201314.","DOI":"10.1038\/s41568-018-0020-9"}],"container-title":["Viruses"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1999-4915\/10\/12\/699\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T15:32:13Z","timestamp":1760196733000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1999-4915\/10\/12\/699"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,12,8]]},"references-count":122,"journal-issue":{"issue":"12","published-online":{"date-parts":[[2018,12]]}},"alternative-id":["v10120699"],"URL":"https:\/\/doi.org\/10.3390\/v10120699","relation":{"has-preprint":[{"id-type":"doi","id":"10.20944\/preprints201811.0475.v1","asserted-by":"object"}]},"ISSN":["1999-4915"],"issn-type":[{"value":"1999-4915","type":"electronic"}],"subject":[],"published":{"date-parts":[[2018,12,8]]}}}