{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,24]],"date-time":"2026-02-24T07:40:14Z","timestamp":1771918814165,"version":"3.50.1"},"reference-count":191,"publisher":"MDPI AG","issue":"2","license":[{"start":{"date-parts":[[2018,2,13]],"date-time":"2018-02-13T00:00:00Z","timestamp":1518480000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000925","name":"NHMRC","doi-asserted-by":"publisher","award":["APP1130512"],"award-info":[{"award-number":["APP1130512"]}],"id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Viruses"],"abstract":"<jats:p>Actin filaments, microtubules and intermediate filaments form the cytoskeleton of vertebrate cells. Involved in maintaining cell integrity and structure, facilitating cargo and vesicle transport, remodelling surface structures and motility, the cytoskeleton is necessary for the successful life of a cell. Because of the broad range of functions these filaments are involved in, they are common targets for viral pathogens, including the alphaherpesviruses. Human-tropic alphaherpesviruses are prevalent pathogens carried by more than half of the world\u2019s population; comprising herpes simplex virus (types 1 and 2) and varicella-zoster virus, these viruses are characterised by their ability to establish latency in sensory neurons. This review will discuss the known mechanisms involved in subversion of and transport via the cytoskeleton during alphaherpesvirus infections, focusing on protein-protein interactions and pathways that have recently been identified. Studies on related alphaherpesviruses whose primary host is not human, along with comparisons to more distantly related beta and gammaherpesviruses, are also presented in this review. The need to decipher as-yet-unknown mechanisms exploited by viruses to hijack cytoskeletal components\u2014to reveal the hidden cytoskeletons in the closet\u2014will also be addressed.<\/jats:p>","DOI":"10.3390\/v10020079","type":"journal-article","created":{"date-parts":[[2018,2,13]],"date-time":"2018-02-13T05:32:19Z","timestamp":1518499939000},"page":"79","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":28,"title":["Cytoskeletons in the Closet\u2014Subversion in Alphaherpesvirus Infections"],"prefix":"10.3390","volume":"10","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8669-8088","authenticated-orcid":false,"given":"Christopher","family":"Denes","sequence":"first","affiliation":[{"name":"Centre for Virus Research, The Westmead Institute for Medical Research, The University of Sydney, Westmead, NSW 2145, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Monica","family":"Miranda-Saksena","sequence":"additional","affiliation":[{"name":"Centre for Virus Research, The Westmead Institute for Medical Research, The University of Sydney, Westmead, NSW 2145, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6744-5667","authenticated-orcid":false,"given":"Anthony","family":"Cunningham","sequence":"additional","affiliation":[{"name":"Centre for Virus Research, The Westmead Institute for Medical Research, The University of Sydney, Westmead, NSW 2145, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8433-4336","authenticated-orcid":false,"given":"Russell","family":"Diefenbach","sequence":"additional","affiliation":[{"name":"Centre for Virus Research, The Westmead Institute for Medical Research, The University of Sydney, Westmead, NSW 2145, Australia"},{"name":"Department of Biomedical Sciences, Faculty of Medicine and Health Sciences, Macquarie University, Sydney, NSW 2109, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2018,2,13]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1208","DOI":"10.1126\/science.1175862","article-title":"Actin, a central player in cell shape and movement","volume":"326","author":"Pollard","year":"2009","journal-title":"Science"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1007\/164_2016_44","article-title":"What We Know and Do Not Know About Actin","volume":"235","author":"Pollard","year":"2017","journal-title":"Handb. Exp. Pharmacol."},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Pollard, T.D. (2016). Actin and Actin-Binding Proteins. Cold Spring Harb. Perspect. Biol., 8.","DOI":"10.1101\/cshperspect.a018226"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"3012","DOI":"10.1242\/dev.153171","article-title":"Microtubule organization, dynamics and functions in differentiated cells","volume":"144","author":"Muroyama","year":"2017","journal-title":"Development"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"562","DOI":"10.1038\/nrm2197","article-title":"Intermediate filaments: From cell architecture to nanomechanics","volume":"8","author":"Herrmann","year":"2007","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_6","unstructured":"Goldmann, W.H. (2017). Intermediate Filaments and Cellular Mechanics. Cell Biol. Int."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1007\/164_2016_41","article-title":"Viruses That Exploit Actin-Based Motility for Their Replication and Spread","volume":"235","author":"Marzook","year":"2017","journal-title":"Handb. Exp. Pharmacol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"107","DOI":"10.3389\/fcimb.2016.00107","article-title":"Hijacking Host Cell Highways: Manipulation of the Host Actin Cytoskeleton by Obligate Intracellular Bacterial Pathogens","volume":"6","author":"Colonne","year":"2016","journal-title":"Front. Cell Infect. Microbiol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.mib.2016.11.007","article-title":"Actin-based motility and cell-to-cell spread of bacterial pathogens","volume":"35","author":"Lamason","year":"2017","journal-title":"Curr. Opin. Microbiol."},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Naghavi, M.H., and Walsh, D. (2017). Microtubule Regulation and Function during Virus Infection. J. Virol., 91.","DOI":"10.1128\/JVI.00538-17"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1515\/bmc-2012-0030","article-title":"Modulation of host microtubule dynamics by pathogenic bacteria","volume":"3","author":"Radhakrishnan","year":"2012","journal-title":"Biomol. Concepts"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1007\/s00705-008-0278-4","article-title":"The order Herpesvirales","volume":"154","author":"Davison","year":"2009","journal-title":"Arch. Virol."},{"key":"ref_13","unstructured":"Knipe, D.M., and Howley, P.M. (2013). Herpesviridae. Fields Virology, Lippincott Williams & Wilkins. [6th ed.]."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1002\/rmv.560","article-title":"Transport and egress of herpes simplex virus in neurons","volume":"18","author":"Diefenbach","year":"2008","journal-title":"Rev. Med. Virol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"9773","DOI":"10.1073\/pnas.85.24.9773","article-title":"Patterns of gene expression and sites of latency in human nerve ganglia are different for varicella-zoster and herpes simplex viruses","volume":"85","author":"Croen","year":"1988","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"R119","DOI":"10.1186\/cc6175","article-title":"Clinical relevance of and risk factors for HSV-related tracheobronchitis or pneumonia: Results of an outbreak investigation","volume":"11","author":"Engelmann","year":"2007","journal-title":"Crit. Care"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1002\/rmv.478","article-title":"Herpes simplex virus and varicella-zoster virus: Why do these human alphaherpesviruses behave so differently from one another?","volume":"15","author":"Mori","year":"2005","journal-title":"Rev. Med. Virol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1159\/000060313","article-title":"Genomic structure and organization of varicella-zoster virus","volume":"3","author":"Cohen","year":"1999","journal-title":"Contrib. Microbiol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1002\/rmv.409","article-title":"Herpes simplex virus gene products: The accessories reflect her lifestyle well","volume":"14","author":"Nishiyama","year":"2004","journal-title":"Rev. Med. Virol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1015","DOI":"10.3390\/v3071015","article-title":"Herpesviruses and intermediate filaments: Close encounters with the third type","volume":"3","author":"Hertel","year":"2011","journal-title":"Viruses"},{"key":"ref_21","first-page":"189","article-title":"Varicella-zoster virus T cell tropism and the pathogenesis of skin infection","volume":"342","author":"Arvin","year":"2010","journal-title":"Curr. Top. Microbiol. Immunol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"S19","DOI":"10.1016\/j.antiviral.2004.06.004","article-title":"HSV shedding","volume":"63","author":"Sacks","year":"2004","journal-title":"Antivir. Res."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"S108","DOI":"10.1111\/j.1600-6143.2009.02901.x","article-title":"Varicella zoster virus (VZV) in solid organ transplant recipients","volume":"9","author":"Pergam","year":"2009","journal-title":"Am. J. Transplant."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1016\/S0966-842X(00)01824-2","article-title":"Mechanisms of viral transport in the cytoplasm","volume":"8","author":"Sodeik","year":"2000","journal-title":"Trends Microbiol."},{"key":"ref_25","first-page":"1635","article-title":"Human herpes simplex virus: Life cycle and development of inhibitors","volume":"79","author":"Kukhanova","year":"2014","journal-title":"Biochemistry"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/ijos.2016.3","article-title":"New strategies against drug resistance to herpes simplex virus","volume":"8","author":"Jiang","year":"2016","journal-title":"Int. J. Oral Sci."},{"key":"ref_27","first-page":"207","article-title":"Oncolytic virotherapy using herpes simplex virus: How far have we come?","volume":"4","author":"Sokolowski","year":"2015","journal-title":"Oncolytic Virother."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.coviro.2016.08.007","article-title":"Retargeting of herpes simplex virus (HSV) vectors","volume":"21","author":"Goins","year":"2016","journal-title":"Curr. Opin. Virol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1016\/j.virusres.2009.03.018","article-title":"Herpesvirus assembly: An update","volume":"143","author":"Mettenleiter","year":"2009","journal-title":"Virus Res."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"5697","DOI":"10.1128\/JVI.75.12.5697-5702.2001","article-title":"Herpes simplex virus nucleocapsids mature to progeny virions by an envelopment \u27f6 deenvelopment \u27f6 reenvelopment pathway","volume":"75","author":"Skepper","year":"2001","journal-title":"J. Virol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"5084","DOI":"10.3390\/v7092861","article-title":"Tegument assembly and secondary envelopment of alphaherpesviruses","volume":"7","author":"Owen","year":"2015","journal-title":"Viruses"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"382","DOI":"10.1038\/nrmicro2559","article-title":"Herpesviruses remodel host membranes for virus egress","volume":"9","author":"Johnson","year":"2011","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1146\/annurev-micro-092611-150051","article-title":"Herpesvirus transport to the nervous system and back again","volume":"66","author":"Smith","year":"2012","journal-title":"Annu. Rev. Microbiol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1007\/978-3-319-53168-7_8","article-title":"Assembly and Egress of an Alphaherpesvirus Clockwork","volume":"223","author":"Smith","year":"2017","journal-title":"Adv. Anat. Embryol. Cell Biol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"678","DOI":"10.3390\/v5020678","article-title":"Directional spread of alphaherpesviruses in the nervous system","volume":"5","author":"Kramer","year":"2013","journal-title":"Viruses"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1016\/j.virusres.2015.09.007","article-title":"Conserved tegument protein complexes: Essential components in the assembly of herpesviruses","volume":"210","author":"Diefenbach","year":"2015","journal-title":"Virus Res."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/j.virusres.2009.07.007","article-title":"Functional roles of the tegument proteins of herpes simplex virus type 1","volume":"145","author":"Kelly","year":"2009","journal-title":"Virus Res."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"5832","DOI":"10.1073\/pnas.0500803102","article-title":"Targeting of herpesvirus capsid transport in axons is coupled to association with specific sets of tegument proteins","volume":"102","author":"Luxton","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"3200","DOI":"10.1128\/JVI.79.5.3200-3205.2005","article-title":"Entry of pseudorabies virus: An immunogold-labeling study","volume":"79","author":"Granzow","year":"2005","journal-title":"J. Virol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1504","DOI":"10.1128\/JVI.02029-09","article-title":"Retrograde axon transport of herpes simplex virus and pseudorabies virus: A live-cell comparative analysis","volume":"84","author":"Antinone","year":"2010","journal-title":"J. Virol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1007","DOI":"10.1083\/jcb.136.5.1007","article-title":"Microtubule-mediated transport of incoming herpes simplex virus 1 capsids to the nucleus","volume":"136","author":"Sodeik","year":"1997","journal-title":"J. Cell Biol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1111\/cmi.12075","article-title":"Cytosolic herpes simplex virus capsids not only require binding inner tegument protein pUL36 but also pUL37 for active transport prior to secondary envelopment","volume":"15","author":"Sandbaumhuter","year":"2013","journal-title":"Cell. Microbiol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"5368","DOI":"10.1128\/JVI.03167-15","article-title":"Conserved Tryptophan Motifs in the Large Tegument Protein pUL36 Are Required for Efficient Secondary Envelopment of Herpes Simplex Virus Capsids","volume":"90","author":"Ivanova","year":"2016","journal-title":"J. Virol."},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Miranda-Saksena, M., Denes, C.E., Diefenbach, R.J., and Cunningham, A.L. (2018). Infection and transport of herpes simplex virus type 1 in neurons: role of the cytoskeleton. Viruses, submitted for publication.","DOI":"10.3390\/v10020092"},{"key":"ref_45","first-page":"917","article-title":"Intracellular transport based on actin polymerization","volume":"79","author":"Khaitlina","year":"2014","journal-title":"Biochemistry"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1083\/jcb.67.1.231","article-title":"Evidence for biased bidirectional polymerization of actin-filaments using heavy-meromyosin prepared by an improved method","volume":"67","author":"Woodrum","year":"1975","journal-title":"J. Cell Biol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"402","DOI":"10.4161\/cam.5.5.16971","article-title":"Filopodia initiation: Focus on the Arp2\/3 complex and formins","volume":"5","author":"Yang","year":"2011","journal-title":"Cell Adh. Migr."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1083\/jcb.127.1.107","article-title":"Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin-agarose","volume":"127","author":"Machesky","year":"1994","journal-title":"J. Cell Biol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"6181","DOI":"10.1073\/pnas.95.11.6181","article-title":"The interaction of Arp2\/3 complex with actin: Nucleation, high affinity pointed end capping, and formation of branching networks of filaments","volume":"95","author":"Mullins","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1016\/S0092-8674(03)00120-X","article-title":"Cellular motility driven by assembly and disassembly of actin filaments","volume":"112","author":"Pollard","year":"2003","journal-title":"Cell"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"768","DOI":"10.1016\/S0959-440X(02)00396-2","article-title":"Structure and function of the Arp2\/3 complex","volume":"12","author":"Pollard","year":"2002","journal-title":"Curr. Opin. Struct. Biol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"2456","DOI":"10.1126\/science.1063025","article-title":"Structure of Arp2\/3 complex in its activated state and in actin filament branch junctions","volume":"293","author":"Volkmann","year":"2001","journal-title":"Science"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"701","DOI":"10.1016\/j.chembiol.2013.03.019","article-title":"Small molecules CK-666 and CK-869 inhibit actin-related protein 2\/3 complex by blocking an activating conformational change","volume":"20","author":"Hetrick","year":"2013","journal-title":"Chem. Biol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1083\/jcb.200709092","article-title":"The structural basis of actin filament branching by the Arp2\/3 complex","volume":"180","author":"Rouiller","year":"2008","journal-title":"J. Cell Biol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"2575","DOI":"10.1242\/jcs.023879","article-title":"WASP and SCAR\/WAVE proteins: The drivers of actin assembly","volume":"122","author":"Pollitt","year":"2009","journal-title":"J. Cell Sci."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/j.molcel.2004.09.018","article-title":"Critical conformational changes in the Arp2\/3 complex are induced by nucleotide and nucleation promoting factor","volume":"16","author":"Goley","year":"2004","journal-title":"Mol. Cell"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1006\/bbrc.1997.8064","article-title":"Direct binding of the verprolin-homology domain in N-WASP to actin is essential for cytoskeletal reorganization","volume":"243","author":"Miki","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1038\/nrmicro2574","article-title":"Subversion of the actin cytoskeleton during viral infection","volume":"9","author":"Taylor","year":"2011","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1126\/science.281.5373.105","article-title":"Interaction of human Arp2\/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation","volume":"281","author":"Welch","year":"1998","journal-title":"Science"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/S0960-9822(99)80020-7","article-title":"Tyrosine phosphorylation is required for actin-based motility of vaccinia but not Listeria or Shigella","volume":"9","author":"Frischknecht","year":"1999","journal-title":"Curr. Biol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"7084","DOI":"10.1128\/JVI.00463-12","article-title":"Replication of herpes simplex virus: Egress of progeny virus at specialized cell membrane sites","volume":"86","author":"Mingo","year":"2012","journal-title":"J. Virol."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/j.neulet.2008.05.031","article-title":"Herpes simplex virus type 1 induces filopodia in differentiated P19 neural cells to facilitate viral spread","volume":"440","author":"Dixit","year":"2008","journal-title":"Neurosci. Lett."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"1396","DOI":"10.1126\/science.1090284","article-title":"Three-dimensional structure of herpes simplex virus from cryo-electron tomography","volume":"302","author":"Grunewald","year":"2003","journal-title":"Science"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"8605","DOI":"10.1128\/JVI.00904-08","article-title":"Comprehensive Characterization of Extracellular Herpes Simplex Virus Type 1 Virions","volume":"82","author":"Loret","year":"2008","journal-title":"J. Virol."},{"key":"ref_65","doi-asserted-by":"crossref","unstructured":"Feierbach, B., Piccinotti, S., Bisher, M., Denk, W., and Enquist, L.W. (2006). Alpha-herpesvirus infection induces the formation of nuclear actin filaments. PLoS Pathog., 2.","DOI":"10.1371\/journal.ppat.0020085"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"2821","DOI":"10.1128\/JVI.01821-07","article-title":"Egress of light particles among filopodia on the surface of Varicella-Zoster virus-infected cells","volume":"82","author":"Carpenter","year":"2008","journal-title":"J. Virol."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1159\/000085100","article-title":"Varicella-zoster virus infection influences expression and organization of actin and alpha-tubulin but does not affect lamin A and vimentin","volume":"48","author":"Kuhn","year":"2005","journal-title":"Intervirology"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1515\/pjvs-2015-0014","article-title":"Equid herpesvirus type 1 (EHV-1) disrupts actin cytoskeleton during productive infection in equine leukocytes","volume":"18","author":"Drebert","year":"2015","journal-title":"Pol. J. Vet. Sci."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"1341","DOI":"10.1007\/s00705-013-1949-3","article-title":"Equine herpesvirus type 1 (EHV-1)-induced rearrangements of actin filaments in productively infected primary murine neurons","volume":"159","author":"Slonska","year":"2014","journal-title":"Arch. Virol."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"336","DOI":"10.3390\/v3040336","article-title":"Actin in herpesvirus infection","volume":"3","author":"Roberts","year":"2011","journal-title":"Viruses"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1016\/j.bbrc.2009.11.027","article-title":"A role for heparan sulfate in viral surfing","volume":"391","author":"Oh","year":"2010","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"6673","DOI":"10.1128\/JVI.00636-15","article-title":"Dynasore disrupts trafficking of herpes simplex virus proteins","volume":"89","author":"Mues","year":"2015","journal-title":"J. Virol."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1016\/j.antiviral.2010.11.012","article-title":"Pentagalloylglucose downregulates cofilin1 and inhibits HSV-1 infection","volume":"89","author":"Pei","year":"2011","journal-title":"Antivir. Res."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"8440","DOI":"10.1128\/JVI.00609-12","article-title":"Cofilin 1-mediated biphasic F-actin dynamics of neuronal cells affect herpes simplex virus 1 infection and replication","volume":"86","author":"Xiang","year":"2012","journal-title":"J. Virol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"9759","DOI":"10.1128\/JVI.00835-09","article-title":"Impact of Rac1 and Cdc42 signaling during early herpes simplex virus type 1 infection of keratinocytes","volume":"83","author":"Petermann","year":"2009","journal-title":"J. Virol."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"3483","DOI":"10.1099\/vir.0.82231-0","article-title":"Early herpes simplex virus type 1 infection is dependent on regulated Rac1\/Cdc42 signalling in epithelial MDCKII cells","volume":"87","author":"Hoppe","year":"2006","journal-title":"J. Gen. Virol."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1016\/j.ceb.2007.09.007","article-title":"The roles of nectins in cell adhesions: Cooperation with other cell adhesion molecules and growth factor receptors","volume":"19","author":"Sakisaka","year":"2007","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"1009","DOI":"10.1083\/jcb.200509155","article-title":"A novel role for phagocytosis-like uptake in herpes simplex virus entry","volume":"174","author":"Clement","year":"2006","journal-title":"J. Cell Biol."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"41","DOI":"10.2174\/1874357901307010041","article-title":"Role of Filopodia in HSV-1 Entry into Zebrafish 3-O-Sulfotransferase-3-Expressing Cells","volume":"7","author":"Choudhary","year":"2013","journal-title":"Open Virol. J."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"13378","DOI":"10.1128\/JVI.03631-13","article-title":"Herpes simplex virus internalization into epithelial cells requires Na+\/H+ exchangers and p21-activated kinases but neither clathrin- nor caveolin-mediated endocytosis","volume":"88","author":"Devadas","year":"2014","journal-title":"J. Virol."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"8990","DOI":"10.1073\/pnas.0409099102","article-title":"Cytoskeletal rearrangements and cell extensions induced by the US3 kinase of an alphaherpesvirus are associated with enhanced spread","volume":"102","author":"Favoreel","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/j.virol.2008.11.050","article-title":"The kinase activity of pseudorabies virus US3 is required for modulation of the actin cytoskeleton","volume":"385","author":"Deruelle","year":"2009","journal-title":"Virology"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"8707","DOI":"10.1073\/pnas.0900436106","article-title":"Alphaherpesvirus US3-mediated reorganization of the actin cytoskeleton is mediated by group A p21-activated kinases","volume":"106","author":"Radu","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.virol.2009.11.012","article-title":"Analysis of filamentous process induction and nuclear localization properties of the HSV-2 serine\/threonine kinase Us3","volume":"397","author":"Finnen","year":"2010","journal-title":"Virology"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1016\/j.vetmic.2015.03.023","article-title":"Pseudorabies virus US3 leads to filamentous actin disassembly and contributes to viral genome delivery to the nucleus","volume":"177","author":"Jacob","year":"2015","journal-title":"Vet. Microbiol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"2328","DOI":"10.1099\/vir.0.000152","article-title":"Pseudorabies virus US3 triggers RhoA phosphorylation to reorganize the actin cytoskeleton","volume":"96","author":"Jacob","year":"2015","journal-title":"J. Gen. Virol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"S22","DOI":"10.1097\/ICO.0b013e3182a0a320","article-title":"Us3, a multifunctional protein kinase encoded by herpes simplex virus 1: How does it function in vivo?","volume":"32","author":"Kawaguchi","year":"2013","journal-title":"Cornea"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"291","DOI":"10.4161\/viru.1.4.11980","article-title":"Subcellular localization of the alphaherpesvirus serine\/threonine kinase Us3 as a determinant of Us3 function","volume":"1","author":"Finnen","year":"2010","journal-title":"Virulence"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"3987","DOI":"10.1128\/JVI.79.7.3987-3997.2005","article-title":"The protein encoded by the US3 orthologue of Marek's disease virus is required for efficient de-envelopment of perinuclear virions and involved in actin stress fiber breakdown","volume":"79","author":"Schumacher","year":"2005","journal-title":"J. Virol."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1016\/j.vetmic.2011.05.037","article-title":"Effect of the US3 protein of bovine herpesvirus 5 on the actin cytoskeleton and apoptosis","volume":"153","author":"Ladelfa","year":"2011","journal-title":"Vet. Microbiol."},{"key":"ref_91","doi-asserted-by":"crossref","unstructured":"Proft, A., Spiesschaert, B., Izume, S., Taferner, S., Lehmann, M.J., and Azab, W. (2016). The Role of the Equine Herpesvirus Type 1 (EHV-1) US3-Encoded Protein Kinase in Actin Reorganization and Nuclear Egress. Viruses, 8.","DOI":"10.3390\/v8100275"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1016\/j.virusres.2010.11.003","article-title":"Role of group A p21-activated kinases in the anti-apoptotic activity of the pseudorabies virus US3 protein kinase","volume":"155","author":"Radu","year":"2011","journal-title":"Virus Res."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"10945","DOI":"10.1128\/JVI.01577-16","article-title":"The US3 Protein of Pseudorabies Virus Drives Viral Passage across the Basement Membrane in Porcine Respiratory Mucosa Explants","volume":"90","author":"Lamote","year":"2016","journal-title":"J. Virol."},{"key":"ref_94","doi-asserted-by":"crossref","unstructured":"Richerioux, N., Blondeau, C., Wiedemann, A., Remy, S., Vautherot, J.F., and Denesvre, C. (2012). Rho-ROCK and Rac-PAK signaling pathways have opposing effects on the cell-to-cell spread of Marek\u2019s Disease Virus. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0044072"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1007\/164_2016_29","article-title":"Myosins: Domain Organisation, Motor Properties, Physiological Roles and Cellular Functions","volume":"235","author":"Masters","year":"2017","journal-title":"Handb. Exp. Pharmacol."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"1627","DOI":"10.1242\/jcs.094300","article-title":"The myosin superfamily at a glance","volume":"125","author":"Hartman","year":"2012","journal-title":"J. Cell Sci."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1002\/ar.10160","article-title":"Myosin superfamily evolutionary history","volume":"268","author":"Thompson","year":"2002","journal-title":"Anat. Rec."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"9889","DOI":"10.1128\/JVI.00732-10","article-title":"Myosin Va enhances secretion of herpes simplex virus 1 virions and cell surface expression of viral glycoproteins","volume":"84","author":"Roberts","year":"2010","journal-title":"J. Virol."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"3471","DOI":"10.1128\/JVI.76.7.3471-3481.2002","article-title":"Evidence of a role for nonmuscle myosin II in herpes simplex virus type 1 egress","volume":"76","author":"Elliott","year":"2002","journal-title":"J. Virol."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"15","DOI":"10.3851\/IMP2661","article-title":"Inhibition of myosin light chain kinase can be targeted for the development of new therapies against herpes simplex virus type-1 infection","volume":"19","author":"Antoine","year":"2014","journal-title":"Antivir. Ther."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"859","DOI":"10.1038\/nature09420","article-title":"Non-muscle myosin IIA is a functional entry receptor for herpes simplex virus-1","volume":"467","author":"Arii","year":"2010","journal-title":"Nature"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"1879","DOI":"10.1128\/JVI.03079-14","article-title":"Nonmuscle myosin heavy chain IIb mediates herpes simplex virus 1 entry","volume":"89","author":"Arii","year":"2015","journal-title":"J. Virol."},{"key":"ref_103","doi-asserted-by":"crossref","unstructured":"Greene, W., and Gao, S.J. (2009). Actin dynamics regulate multiple endosomal steps during Kaposi\u2019s sarcoma-associated herpesvirus entry and trafficking in endothelial cells. PLoS Pathog., 5.","DOI":"10.1371\/journal.ppat.1000512"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1016\/j.chom.2014.07.005","article-title":"HCMV pUL135 remodels the actin cytoskeleton to impair immune recognition of infected cells","volume":"16","author":"Stanton","year":"2014","journal-title":"Cell Host Microbe"},{"key":"ref_105","doi-asserted-by":"crossref","unstructured":"Wilkie, A.R., Lawler, J.L., and Coen, D.M. (2016). A role for nuclear F-actin induction in human cytomegalovirus nuclear egress. MBio, 7.","DOI":"10.1128\/mBio.01254-16"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"E5725","DOI":"10.1073\/pnas.1513876112","article-title":"Remodeling nuclear architecture allows efficient transport of herpesvirus capsids by diffusion","volume":"112","author":"Bosse","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"e01909","DOI":"10.1128\/mBio.01909-14","article-title":"Nuclear herpesvirus capsid motility is not dependent on F-actin","volume":"5","author":"Bosse","year":"2014","journal-title":"MBio"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1016\/j.cels.2016.08.012","article-title":"A Portrait of the Human Organelle Proteome In Space and Time during Cytomegalovirus Infection","volume":"3","author":"Mathias","year":"2016","journal-title":"Cell Syst."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"410","DOI":"10.4149\/av_2016_04_410","article-title":"Function of myosin during entry and egress of equid herpesvirus type 1 in primary murine neurons","volume":"60","author":"Cymerys","year":"2016","journal-title":"Acta Virol."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"448","DOI":"10.15252\/embj.201490358","article-title":"KSHV-TK is a tyrosine kinase that disrupts focal adhesions and induces Rho-mediated cell contraction","volume":"34","author":"Gill","year":"2015","journal-title":"EMBO J."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"1332","DOI":"10.1128\/JVI.80.3.1332-1339.2006","article-title":"Composition of pseudorabies virus particles lacking tegument protein US3, UL47, or UL49 or envelope glycoprotein E","volume":"80","author":"Michael","year":"2006","journal-title":"J. Virol."},{"key":"ref_112","unstructured":"Alberts, B., Johnson, A., Lewis, J., Morgan, D., Raff, M., Roberts, K., and Walter, P. (2015). Molecular Biology of the Cell, Garland Science. [6th ed.]."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"879","DOI":"10.1038\/nature09207","article-title":"Microtubule nucleating gamma-TuSC assembles structures with 13-fold microtubule-like symmetry","volume":"466","author":"Kollman","year":"2010","journal-title":"Nature"},{"key":"ref_114","doi-asserted-by":"crossref","unstructured":"Manning, J.A., Shalini, S., Risk, J.M., Day, C.L., and Kumar, S. (2010). A direct interaction with NEDD1 regulates gamma-tubulin recruitment to the centrosome. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0009618"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1038\/nrm4084","article-title":"Control of microtubule organization and dynamics: Two ends in the limelight","volume":"16","author":"Akhmanova","year":"2015","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1515\/bmc-2016-0018","article-title":"Role of non-motile microtubule-associated proteins in virus trafficking","volume":"7","author":"Portilho","year":"2016","journal-title":"Biomol. Concepts"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"7102","DOI":"10.1128\/JVI.00764-13","article-title":"Differing effects of herpes simplex virus 1 and pseudorabies virus infections on centrosomal function","volume":"87","author":"Pasdeloup","year":"2013","journal-title":"J. Virol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"8697","DOI":"10.1128\/JVI.75.18.8697-8711.2001","article-title":"Microtubule reorganization during herpes simplex virus type 1 infection facilitates the nuclear localization of VP22, a major virion tegument protein","volume":"75","author":"Kotsakis","year":"2001","journal-title":"J. Virol."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1007\/BF01313722","article-title":"Microtubules and intermediate filaments of herpes simplex virus infected cells","volume":"94","author":"Dienes","year":"1987","journal-title":"Arch. Virol."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1016\/j.vetmic.2010.02.008","article-title":"Point mutations in BHV-1 Us3 gene abolish its ability to induce cytoskeletal changes in various cell types","volume":"143","author":"Brzozowska","year":"2010","journal-title":"Vet. Microbiol."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1083\/jcb.201505123","article-title":"Microtubule plus end-associated CLIP-170 initiates HSV-1 retrograde transport in primary human cells","volume":"211","author":"Jovasevic","year":"2015","journal-title":"J. Cell Biol."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"18268","DOI":"10.1073\/pnas.1310760110","article-title":"Plus-end tracking proteins, CLASPs, and a viral Akt mimic regulate herpesvirus-induced stable microtubule formation and virus spread","volume":"110","author":"Naghavi","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_123","doi-asserted-by":"crossref","unstructured":"Liu, M., Schmidt, E.E., and Halford, W.P. (2010). ICP0 dismantles microtubule networks in herpes simplex virus-infected cells. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0010975"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"1585","DOI":"10.1093\/hmg\/ddr036","article-title":"IKAP\/Elp1 involvement in cytoskeleton regulation and implication for familial dysautonomia","volume":"20","author":"Cheishvili","year":"2011","journal-title":"Hum. Mol. Genet."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1016\/j.bbrc.2011.12.044","article-title":"Identification of host cell proteins which interact with herpes simplex virus type 1 tegument protein pUL37","volume":"417","author":"Kelly","year":"2012","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1099\/vir.0.19530-0","article-title":"Herpes simplex virus type 1 infection of polarized epithelial cells requires microtubules and access to receptors present at cell-cell contact sites","volume":"85","author":"Marozin","year":"2004","journal-title":"J. Gen. Virol."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"9962","DOI":"10.1128\/JVI.76.19.9962-9971.2002","article-title":"Intact microtubules support adenovirus and herpes simplex virus infections","volume":"76","author":"Mabit","year":"2002","journal-title":"J. Virol."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1523\/JNEUROSCI.14-01-00318.1994","article-title":"Microtubule polarity in the peripheral processes of trigeminal ganglion cells: Relevance for the retrograde transport of herpes simplex virus","volume":"14","author":"Topp","year":"1994","journal-title":"J. Neurosci."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"682","DOI":"10.1038\/nrm2774","article-title":"Kinesin superfamily motor proteins and intracellular transport","volume":"10","author":"Hirokawa","year":"2009","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.yexcr.2015.02.016","article-title":"Kinesin superfamily proteins (KIFs): Various functions and their relevance for important phenomena in life and diseases","volume":"334","author":"Hirokawa","year":"2015","journal-title":"Exp. Cell Res."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"4369","DOI":"10.1242\/jcs.03176","article-title":"The dynein family at a glance","volume":"119","author":"Hook","year":"2006","journal-title":"J. Cell Sci."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"1169","DOI":"10.1042\/BST0391169","article-title":"Cytoplasmic dynein","volume":"39","author":"Allan","year":"2011","journal-title":"Biochem. Soc. Trans."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1016\/j.tim.2015.01.002","article-title":"Axonal spread of neuroinvasive viral infections","volume":"23","author":"Taylor","year":"2015","journal-title":"Trends Microbiol."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1016\/j.tim.2005.05.010","article-title":"Viral stop-and-go along microtubules: Taking a ride with dynein and kinesins","volume":"13","author":"Dohner","year":"2005","journal-title":"Trends Microbiol."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"3527","DOI":"10.1038\/emboj.2011.283","article-title":"Coupling viruses to dynein and kinesin-1","volume":"30","author":"Dodding","year":"2011","journal-title":"EMBO J."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"3466","DOI":"10.1073\/pnas.061029798","article-title":"Herpesviruses use bidirectional fast-axonal transport to spread in sensory neurons","volume":"98","author":"Smith","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1083\/jcb.200408113","article-title":"A standardized kinesin nomenclature","volume":"167","author":"Lawrence","year":"2004","journal-title":"J. Cell Biol."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1038\/nrm3667","article-title":"Functions and mechanics of dynein motor proteins","volume":"14","author":"Roberts","year":"2013","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.tibs.2015.11.004","article-title":"How Dynein Moves Along Microtubules","volume":"41","author":"Bhabha","year":"2016","journal-title":"Trends Biochem. Sci."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"1355","DOI":"10.1128\/JVI.74.3.1355-1363.2000","article-title":"The herpes simplex virus 1 U(L)34 protein interacts with a cytoplasmic dynein intermediate chain and targets nuclear membrane","volume":"74","author":"Ye","year":"2000","journal-title":"J. Virol."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"3282","DOI":"10.1128\/JVI.76.7.3282-3291.2002","article-title":"Herpes simplex virus tegument protein US11 interacts with conventional kinesin heavy chain","volume":"76","author":"Diefenbach","year":"2002","journal-title":"J. Virol."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"7388","DOI":"10.1128\/JVI.00225-08","article-title":"UL36p is required for efficient transport of membrane-associated herpes simplex virus type 1 along microtubules","volume":"82","author":"Shanda","year":"2008","journal-title":"J. Virol."},{"key":"ref_143","doi-asserted-by":"crossref","unstructured":"Radtke, K., Kieneke, D., Wolfstein, A., Michael, K., Steffen, W., Scholz, T., Karger, A., and Sodeik, B. (2010). Plus- and minus-end directed microtubule motors bind simultaneously to herpes simplex virus capsids using different inner tegument structures. PLoS Pathog., 6.","DOI":"10.1371\/journal.ppat.1000991"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/j.chom.2013.01.009","article-title":"The herpesvirus VP1\/2 protein is an effector of dynein-mediated capsid transport and neuroinvasion","volume":"13","author":"Zaichick","year":"2013","journal-title":"Cell Host Microbe"},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"2857","DOI":"10.1128\/JVI.02676-12","article-title":"Herpesvirus tegument protein pUL37 interacts with dystonin\/BPAG1 to promote capsid transport on microtubules during egress","volume":"87","author":"Pasdeloup","year":"2013","journal-title":"J. Virol."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"11008","DOI":"10.1128\/JVI.01633-13","article-title":"Dystonin\/BPAG1 promotes plus-end-directed transport of herpes simplex virus 1 capsids on microtubules during entry","volume":"87","author":"McElwee","year":"2013","journal-title":"J. Virol."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"2102","DOI":"10.1128\/JVI.03041-15","article-title":"The Basic Domain of Herpes Simplex Virus 1 pUS9 Recruits Kinesin-1 To Facilitate Egress from Neurons","volume":"90","author":"Diefenbach","year":"2016","journal-title":"J. Virol."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"8088","DOI":"10.1128\/JVI.00771-15","article-title":"Pseudorabies Virus Fast Axonal Transport Occurs by a pUS9-Independent Mechanism","volume":"89","author":"Daniel","year":"2015","journal-title":"J. Virol."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"806","DOI":"10.1016\/j.chom.2012.10.013","article-title":"Kinesin-3 mediates axonal sorting and directional transport of alphaherpesvirus particles in neurons","volume":"12","author":"Kramer","year":"2012","journal-title":"Cell Host Microbe"},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"8211","DOI":"10.1128\/JVI.02528-05","article-title":"Eclipse phase of herpes simplex virus type 1 infection: Efficient dynein-mediated capsid transport without the small capsid protein VP26","volume":"80","author":"Dohner","year":"2006","journal-title":"J. Virol."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"5494","DOI":"10.1128\/JVI.00026-06","article-title":"The Herpesvirus capsid surface protein, VP26, and the majority of the tegument proteins are dispensable for capsid transport toward the nucleus","volume":"80","author":"Antinone","year":"2006","journal-title":"J. Virol."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"28522","DOI":"10.1074\/jbc.M311671200","article-title":"Herpes simplex virus type 1 capsid protein VP26 interacts with dynein light chains RP3 and Tctex1 and plays a role in retrograde cellular transport","volume":"279","author":"Douglas","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/j.virol.2015.11.014","article-title":"The pseudorabies virus protein, pUL56, enhances virus dissemination and virulence but is dispensable for axonal transport","volume":"488","author":"Daniel","year":"2016","journal-title":"Virology"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1099\/vir.0.80633-0","article-title":"Herpes simplex virus type 2 membrane protein UL56 associates with the kinesin motor protein KIF1A","volume":"86","author":"Koshizuka","year":"2005","journal-title":"J. Gen. Virol."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1128\/JVI.80.1.201-209.2006","article-title":"The pseudorabies virus VP1\/2 tegument protein is required for intracellular capsid transport","volume":"80","author":"Luxton","year":"2006","journal-title":"J. Virol."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1111\/j.1600-0854.2005.00379.x","article-title":"The inner tegument promotes herpes simplex virus capsid motility along microtubules in vitro","volume":"7","author":"Wolfstein","year":"2006","journal-title":"Traffic"},{"key":"ref_157","doi-asserted-by":"crossref","unstructured":"Richards, A.L., Sollars, P.J., Pitts, J.D., Stults, A.M., Heldwein, E.E., Pickard, G.E., and Smith, G.E. (2017). The pUL37 tegument protein guides alpha-herpesvirus retrograde axonal transport to promote neuroinvasion. PLoS Pathog.","DOI":"10.1371\/journal.ppat.1006741"},{"key":"ref_158","doi-asserted-by":"crossref","unstructured":"Buch, A., Muller, O., Ivanova, L., Dohner, K., Bialy, D., Bosse, J.B., Pohlmann, A., Binz, A., Hegemann, M., and Nagel, C.H. (2017). Inner tegument proteins of Herpes Simplex Virus are sufficient for intracellular capsid motility in neurons but not for axonal targeting. PLoS Pathog., 13.","DOI":"10.1371\/journal.ppat.1006813"},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1126\/science.1234264","article-title":"Structural basis for kinesin-1:cargo recognition","volume":"340","author":"Pernigo","year":"2013","journal-title":"Science"},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"4523","DOI":"10.1038\/emboj.2011.326","article-title":"A kinesin-1 binding motif in vaccinia virus that is widespread throughout the human genome","volume":"30","author":"Dodding","year":"2011","journal-title":"EMBO J."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"10053","DOI":"10.1074\/jbc.M109.044420","article-title":"Regulation of microtubule dynamics through phosphorylation on stathmin by Epstein-Barr virus kinase BGLF4","volume":"285","author":"Chen","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1247\/csf.24.345","article-title":"Stathmin and its phosphoprotein family: General properties, biochemical and functional interaction with tubulin","volume":"24","author":"Curmi","year":"1999","journal-title":"Cell Struct. Funct."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"1191","DOI":"10.1128\/JVI.79.2.1191-1206.2005","article-title":"Kaposi\u2019s sarcoma-associated herpesvirus modulates microtubule dynamics via RhoA-GTP-diaphanous 2 signaling and utilizes the dynein motors to deliver its DNA to the nucleus","volume":"79","author":"Naranatt","year":"2005","journal-title":"J. Virol."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"9431","DOI":"10.1128\/JVI.01317-13","article-title":"Glycoproteins gE and gI are required for efficient KIF1A-dependent anterograde axonal transport of alphaherpesvirus particles in neurons","volume":"87","author":"Kratchmarov","year":"2013","journal-title":"J. Virol."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1128\/JVI.02465-12","article-title":"Herpes simplex virus membrane proteins gE\/gI and US9 act cooperatively to promote transport of capsids and glycoproteins from neuron cell bodies into initial axon segments","volume":"87","author":"Howard","year":"2013","journal-title":"J. Virol."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"17145","DOI":"10.1074\/jbc.R115.640359","article-title":"Intermediate Filaments Play a Pivotal Role in Regulating Cell Architecture and Function","volume":"290","author":"Lowery","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/j.tcb.2007.11.004","article-title":"Intermediate filament assembly: Dynamics to disease","volume":"18","author":"Godsel","year":"2008","journal-title":"Trends Cell Biol."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1016\/j.jsb.2011.11.017","article-title":"Inroads into the structure and function of intermediate filament networks","volume":"177","author":"Goldman","year":"2012","journal-title":"J. Struct. Biol."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"54","DOI":"10.12703\/P6-54","article-title":"Intermediate filaments: A dynamic network that controls cell mechanics","volume":"6","author":"Gruenbaum","year":"2014","journal-title":"F1000Prime Rep."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1016\/j.tibs.2006.05.008","article-title":"\u201cHeads and tails\u201d of intermediate filament phosphorylation: Multiple sites and functional insights","volume":"31","author":"Omary","year":"2006","journal-title":"Trends Biochem. Sci."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"7015","DOI":"10.1128\/JVI.00398-09","article-title":"Onset of human cytomegalovirus replication in fibroblasts requires the presence of an intact vimentin cytoskeleton","volume":"83","author":"Miller","year":"2009","journal-title":"J. Virol."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"707","DOI":"10.1111\/j.1348-0421.2002.tb02755.x","article-title":"Phosphorylation of cytokeratin 17 by herpes simplex virus type 2 US3 protein kinase","volume":"46","author":"Murata","year":"2002","journal-title":"Microbiol. Immunol."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1099\/0022-1317-68-3-737","article-title":"Herpes simplex virus-induced changes of the keratin type intermediate filament in rat epithelial cells","volume":"68","author":"Forchhammer","year":"1987","journal-title":"J. Gen. Virol."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"5564","DOI":"10.1128\/JVI.78.11.5564-5575.2004","article-title":"Conformational changes in the nuclear lamina induced by herpes simplex virus type 1 require genes U(L)31 and U(L)34","volume":"78","author":"Reynolds","year":"2004","journal-title":"J. Virol."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"854","DOI":"10.1126\/science.1071506","article-title":"Cytomegalovirus recruitment of cellular kinases to dissolve the nuclear lamina","volume":"297","author":"Muranyi","year":"2002","journal-title":"Science"},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"9010","DOI":"10.1073\/pnas.1511140112","article-title":"Structure of a herpesvirus nuclear egress complex subunit reveals an interaction groove that is essential for viral replication","volume":"112","author":"Leigh","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1128\/JVI.02358-13","article-title":"Human cytomegalovirus UL50 and UL53 recruit viral protein kinase UL97, not protein kinase C, for disruption of nuclear lamina and nuclear egress in infected cells","volume":"88","author":"Sharma","year":"2014","journal-title":"J. Virol."},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1111\/cmi.12044","article-title":"The way out: What we know and do not know about herpesvirus nuclear egress","volume":"15","author":"Mettenleiter","year":"2013","journal-title":"Cell. Microbiol."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"8982","DOI":"10.1128\/JVI.01220-15","article-title":"Role of Host Cell p32 in Herpes Simplex Virus 1 De-Envelopment during Viral Nuclear Egress","volume":"89","author":"Liu","year":"2015","journal-title":"J. Virol."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"10414","DOI":"10.1128\/JVI.01392-16","article-title":"Herpes Simplex Virus 1 Induces Phosphorylation and Reorganization of Lamin A\/C through the \u03b3134.5 Protein That Facilitates Nuclear Egress","volume":"90","author":"Wu","year":"2016","journal-title":"J. Virol."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"6459","DOI":"10.1128\/JVI.00380-07","article-title":"US3 of Herpes Simplex Virus Type 1 Encodes a Promiscuous Protein Kinase That Phosphorylates and Alters Localization of Lamin A\/C in Infected Cells","volume":"81","author":"Mou","year":"2007","journal-title":"J. Virol."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/j.virol.2009.06.051","article-title":"Herpes simplex virus 2 UL13 protein kinase disrupts nuclear lamins","volume":"392","author":"Wylie","year":"2009","journal-title":"Virology"},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"4429","DOI":"10.1128\/JVI.02354-06","article-title":"Herpes simplex virus infection induces phosphorylation and delocalization of emerin, a key inner nuclear membrane protein","volume":"81","author":"Morris","year":"2007","journal-title":"J. Virol."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"1268","DOI":"10.1128\/JVI.77.2.1268-1280.2003","article-title":"Microarray analysis of host cell gene transcription in response to varicella-zoster virus infection of human T cells and fibroblasts in vitro and SCIDhu skin xenografts in vivo","volume":"77","author":"Jones","year":"2003","journal-title":"J. Virol."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"17031","DOI":"10.1073\/pnas.252588599","article-title":"The patterns of accumulation of cellular RNAs in cells infected with a wild-type and a mutant herpes simplex virus 1 lacking the virion host shutoff gene","volume":"99","author":"Taddeo","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"3489","DOI":"10.1128\/JVI.78.7.3489-3501.2004","article-title":"Transcriptional response of a common permissive cell type to infection by two diverse alphaherpesviruses","volume":"78","author":"Ray","year":"2004","journal-title":"J. Virol."},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1007\/s00005-015-0382-6","article-title":"Novel Insights into the Roles of Rho Kinase in Cancer","volume":"64","author":"Wei","year":"2016","journal-title":"Arch. Immunol. Ther. Exp."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1038\/bjc.2015.264","article-title":"Hitting the brakes: Targeting microtubule motors in cancer","volume":"113","author":"Chandrasekaran","year":"2015","journal-title":"Br. J. Cancer"},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/j.pneurobio.2016.04.007","article-title":"The cytoskeleton as a novel therapeutic target for old neurodegenerative disorders","volume":"141","author":"Eira","year":"2016","journal-title":"Prog. Neurobiol."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"5716","DOI":"10.1073\/pnas.74.12.5716","article-title":"Selectivity of action of an antiherpetic agent, 9-(2-hydroxyethoxymethyl) guanine","volume":"74","author":"Elion","year":"1977","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_191","first-page":"94","article-title":"Herpesvirus vectors in gene therapy","volume":"4","author":"Hukkanen","year":"2010","journal-title":"Open Virol. J."}],"container-title":["Viruses"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1999-4915\/10\/2\/79\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T14:54:56Z","timestamp":1760194496000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1999-4915\/10\/2\/79"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,2,13]]},"references-count":191,"journal-issue":{"issue":"2","published-online":{"date-parts":[[2018,2]]}},"alternative-id":["v10020079"],"URL":"https:\/\/doi.org\/10.3390\/v10020079","relation":{},"ISSN":["1999-4915"],"issn-type":[{"value":"1999-4915","type":"electronic"}],"subject":[],"published":{"date-parts":[[2018,2,13]]}}}