{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T15:55:24Z","timestamp":1792684524092,"version":"4.5.0"},"reference-count":214,"publisher":"MDPI AG","issue":"12","license":[{"start":{"date-parts":[[2019,12,17]],"date-time":"2019-12-17T00:00:00Z","timestamp":1576540800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["R01 AI125244"],"award-info":[{"award-number":["R01 AI125244"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Viruses"],"abstract":"<jats:p>The Alphaherpesvirinae include the neurotropic pathogens herpes simplex virus and varicella zoster virus of humans and pseudorabies virus of swine. These viruses establish lifelong latency in the nuclei of peripheral ganglia, but utilize the peripheral tissues those neurons innervate for productive replication, spread, and transmission. Delivery of virions from replicative pools to the sites of latency requires microtubule-directed retrograde axonal transport from the nerve terminus to the cell body of the sensory neuron. As a corollary, during reactivation newly assembled virions must travel along axonal microtubules in the anterograde direction to return to the nerve terminus and infect peripheral tissues, completing the cycle. Neurotropic alphaherpesviruses can therefore exploit neuronal microtubules and motors for long distance axonal transport, and alternate between periods of sustained plus end- and minus end-directed motion at different stages of their infectious cycle. This review summarizes our current understanding of the molecular details by which this is achieved.<\/jats:p>","DOI":"10.3390\/v11121165","type":"journal-article","created":{"date-parts":[[2019,12,20]],"date-time":"2019-12-20T03:19:36Z","timestamp":1576811976000},"page":"1165","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":29,"title":["Microtubule-Dependent Trafficking of Alphaherpesviruses in the Nervous System: The Ins and Outs"],"prefix":"10.3390","volume":"11","author":[{"given":"Drishya","family":"Diwaker","sequence":"first","affiliation":[{"name":"Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1238-9407","authenticated-orcid":false,"given":"Duncan W.","family":"Wilson","sequence":"additional","affiliation":[{"name":"Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA"},{"name":"Dominick P. Purpura Department of Neuroscience, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2019,12,17]]},"reference":[{"key":"ref_1","first-page":"1802","article-title":"Herpesviridae","volume":"Volume 2","author":"Knipe","year":"2013","journal-title":"Fields Virology"},{"key":"ref_2","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_3","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_4","doi-asserted-by":"crossref","first-page":"1015","DOI":"10.1016\/S1474-4422(07)70267-3","article-title":"The neurotropic herpes viruses: Herpes simplex and varicella-zoster","volume":"6","author":"Steiner","year":"2007","journal-title":"Lancet Neurol."},{"key":"ref_5","first-page":"1824","article-title":"Herpes simplex viruses","volume":"Volume 2","author":"Knipe","year":"2013","journal-title":"Fields Virology"},{"key":"ref_6","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_7","doi-asserted-by":"crossref","first-page":"462","DOI":"10.1128\/MMBR.69.3.462-500.2005","article-title":"Molecular biology of pseudorabies virus: Impact on neurovirology and veterinary medicine","volume":"69","author":"Pomeranz","year":"2005","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"7609","DOI":"10.1128\/JVI.79.12.7609-7616.2005","article-title":"Herpes simplex virus type 1 enters human epidermal keratinocytes, but not neurons, via a pH-dependent endocytic pathway","volume":"79","author":"Nicola","year":"2005","journal-title":"J. Virol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"16034","DOI":"10.1073\/pnas.0404686101","article-title":"Local modulation of plus-end transport targets herpesvirus entry and egress in sensory axons","volume":"101","author":"Smith","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Denes, C.E., Miranda-Saksena, M., Cunningham, A.L., and Diefenbach, R.J. (2018). Cytoskeletons in the closet-subversion in alphaherpesvirus infections. Viruses, 10.","DOI":"10.3390\/v10020079"},{"key":"ref_11","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, 10.","DOI":"10.3390\/v10020092"},{"key":"ref_12","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_13","doi-asserted-by":"crossref","first-page":"e00392\u201319","DOI":"10.1128\/JVI.00392-19","article-title":"Seeking closure: How do herpesviruses recruit the cellular ESCRT apparatus?","volume":"93","author":"Barnes","year":"2019","journal-title":"J. Virol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1007\/978-981-10-7230-7_2","article-title":"Virus assembly and egress of HSV","volume":"1045","author":"Crump","year":"2018","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1007\/978-3-319-53168-7_6","article-title":"Herpesvirus capsid assembly and DNA packaging","volume":"223","author":"Heming","year":"2017","journal-title":"Adv. Anat. Embryol. Cell Biol."},{"key":"ref_16","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_17","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_18","doi-asserted-by":"crossref","first-page":"1502","DOI":"10.1128\/JVI.02887-14","article-title":"The large tegument protein pUL36 is essential for formation of the capsid vertex-specific component at the capsid-tegument interface of herpes simplex virus 1","volume":"89","author":"Fan","year":"2015","journal-title":"J. Virol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"15827","DOI":"10.1074\/jbc.RA118.004481","article-title":"The dynamic nature of the conserved tegument protein UL37 of herpesviruses","volume":"293","author":"Koenigsberg","year":"2018","journal-title":"J. Biol. Chem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"11790","DOI":"10.1128\/JVI.01113-07","article-title":"The capsid and tegument of the alphaherpesviruses are linked by an interaction between the UL25 and VP1\/2 proteins","volume":"81","author":"Coller","year":"2007","journal-title":"J. Virol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1016\/j.virol.2011.11.002","article-title":"Identification of a single amino acid residue which is critical for the interaction between HSV-1 inner tegument proteins pUL36 and pUL37","volume":"422","author":"Kelly","year":"2012","journal-title":"Virology"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/j.virol.2014.02.003","article-title":"The interaction of the HSV-1 tegument proteins pUL36 and pUL37 is essential for secondary envelopment during viral egress","volume":"454","author":"Kelly","year":"2014","journal-title":"Virology"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.virol.2007.07.005","article-title":"Residues F593 and E596 of HSV-1 tegument protein pUL36 (VP1\/2) mediate binding of tegument protein pUL37","volume":"368","author":"Mijatov","year":"2007","journal-title":"Virology"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"3065","DOI":"10.1128\/JVI.76.6.3065-3071.2002","article-title":"Pseudorabies virus UL36 tegument protein physically interacts with the UL37 protein","volume":"76","author":"Klupp","year":"2002","journal-title":"J. Virol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"9566","DOI":"10.1128\/JVI.79.15.9566-9571.2005","article-title":"Determination of interactions between tegument proteins of herpes simplex virus type 1","volume":"79","author":"Vittone","year":"2005","journal-title":"J. Virol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"5462","DOI":"10.1128\/JVI.00163-14","article-title":"Crystal structure of the herpesvirus inner tegument protein UL37 supports its essential role in control of viral trafficking","volume":"88","author":"Pitts","year":"2014","journal-title":"J. Virol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"e01244-17","DOI":"10.1128\/JVI.01244-17","article-title":"Crystal Structure of the N-terminal half of the traffic controller UL37 from Herpes simplex virus 1","volume":"91","author":"Koenigsberg","year":"2017","journal-title":"J. Virol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"11608","DOI":"10.1128\/JVI.74.24.11608-11618.2000","article-title":"A null mutation in the UL36 gene of herpes simplex virus type 1 results in accumulation of unenveloped DNA-filled capsids in the cytoplasm of infected cells","volume":"74","author":"Desai","year":"2000","journal-title":"J. Virol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"10259","DOI":"10.1128\/JVI.75.21.10259-10271.2001","article-title":"A null mutation in the gene encoding the herpes simplex virus type 1 UL37 polypeptide abrogates virus maturation","volume":"75","author":"Desai","year":"2001","journal-title":"J. Virol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"9408","DOI":"10.1128\/JVI.00361-10","article-title":"Structure and capsid association of the herpesvirus large tegument protein UL36","volume":"84","author":"Newcomb","year":"2010","journal-title":"J. Virol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1397","DOI":"10.1128\/JVI.01721-09","article-title":"The major determinant for addition of tegument protein pUL48 (VP16) to capsids in herpes simplex virus type 1 is the presence of the major tegument protein pUL36 (VP1\/2)","volume":"84","author":"Ko","year":"2010","journal-title":"J. Virol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1128\/JVI.05981-11","article-title":"Analysis of the interaction between the essential herpes simplex virus 1 tegument proteins VP16 and VP1\/2","volume":"86","author":"Svobodova","year":"2012","journal-title":"J. Virol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1099\/vir.0.80444-0","article-title":"The cytoplasmic tail of herpes simplex virus envelope glycoprotein D binds to the tegument protein VP22 and to capsids","volume":"86","author":"Chi","year":"2005","journal-title":"J. Gen. Virol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.virol.2003.08.023","article-title":"The cytoplasmic tail of Herpes simplex virus glycoprotein H binds to the tegument protein VP16 in vitro and in vivo","volume":"317","author":"Gross","year":"2003","journal-title":"Virology"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"6134","DOI":"10.1128\/JVI.79.10.6134-6141.2005","article-title":"Structural basis for the physiological temperature dependence of the association of VP16 with the cytoplasmic tail of herpes simplex virus glycoprotein H","volume":"79","author":"Kamen","year":"2005","journal-title":"J. Virol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1016\/j.virol.2006.08.024","article-title":"A conserved region of the herpes simplex virus type 1 tegument protein VP22 facilitates interaction with the cytoplasmic tail of glycoprotein E (gE)","volume":"358","author":"Bucks","year":"2007","journal-title":"Virology"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"10179","DOI":"10.1128\/JVI.77.19.10179-10185.2003","article-title":"Herpesvirus entry: An update","volume":"77","author":"Spear","year":"2003","journal-title":"J. Virol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1016\/j.semcdb.2017.08.020","article-title":"ESCRT-dependent cargo sorting at multivesicular endosomes","volume":"74","author":"Frankel","year":"2018","journal-title":"Semin. Cell Dev. Biol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"5324","DOI":"10.1128\/JVI.77.9.5324-5332.2003","article-title":"Roles for endocytosis and low pH in herpes simplex virus entry into HeLa and Chinese hamster ovary cells","volume":"77","author":"Nicola","year":"2003","journal-title":"J. Virol."},{"key":"ref_40","doi-asserted-by":"crossref","unstructured":"Piccinotti, S., and Whelan, S.P. (2016). Rabies internalizes into primary peripheral neurons via clathrin coated pits and requires fusion at the cell body. PLoS Pathog., 12.","DOI":"10.1371\/journal.ppat.1005753"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1016\/S0966-842X(01)02200-4","article-title":"Recent insights into poliovirus pathogenesis","volume":"9","author":"Ohka","year":"2001","journal-title":"Trends Microbiol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1016\/j.chom.2013.03.010","article-title":"Virus infections in the nervous system","volume":"13","author":"Koyuncu","year":"2013","journal-title":"Cell Host Microbe"},{"key":"ref_43","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_44","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_45","doi-asserted-by":"crossref","unstructured":"Olenick, M.A., and Holzbaur, E.L.F. (2019). Dynein activators and adaptors at a glance. J. Cell Sci., 132.","DOI":"10.1242\/jcs.227132"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"R320","DOI":"10.1016\/S0960-9822(03)00237-9","article-title":"Dynactin: Coordinating motors with opposite inclinations","volume":"13","author":"Gross","year":"2003","journal-title":"Curr. Biol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"2610","DOI":"10.1016\/j.bpj.2010.02.037","article-title":"Bidirectional transport by molecular motors: Enhanced processivity and response to external forces","volume":"98","author":"Muller","year":"2010","journal-title":"Biophys. J."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1016\/j.chom.2012.10.021","article-title":"Efficient retrograde transport of pseudorabies virus within neurons requires local protein synthesis in axons","volume":"13","author":"Koyuncu","year":"2013","journal-title":"Cell Host Microbe"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1095","DOI":"10.1016\/S0896-6273(03)00770-0","article-title":"Axoplasmic importins enable retrograde injury signaling in lesioned nerve","volume":"40","author":"Hanz","year":"2003","journal-title":"Neuron"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"15113","DOI":"10.1523\/JNEUROSCI.3947-10.2010","article-title":"IL-6- and NGF-induced rapid control of protein synthesis and nociceptive plasticity via convergent signaling to the eIF4F complex","volume":"30","author":"Melemedjian","year":"2010","journal-title":"J. Neurosci."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1016\/j.neuron.2008.05.029","article-title":"Localized regulation of axonal RanGTPase controls retrograde injury signaling in peripheral nerve","volume":"59","author":"Yudin","year":"2008","journal-title":"Neuron"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"784","DOI":"10.1038\/35041020","article-title":"A role for the lissencephaly gene LIS1 in mitosis and cytoplasmic dynein function","volume":"2","author":"Faulkner","year":"2000","journal-title":"Nat. Cell Biol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1038\/35041000","article-title":"Regulation of cytoplasmic dynein behaviour and microtubule organization by mammalian Lis1","volume":"2","author":"Smith","year":"2000","journal-title":"Nat. Cell Biol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1083\/jcb.201104076","article-title":"High-resolution imaging reveals indirect coordination of opposite motors and a role for LIS1 in high-load axonal transport","volume":"195","author":"Yi","year":"2011","journal-title":"J. Cell Biol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1197","DOI":"10.1016\/j.cell.2017.08.037","article-title":"Lis1 has two opposing modes of regulating cytoplasmic dynein","volume":"170","author":"DeSantis","year":"2017","journal-title":"Cell"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"a021642","DOI":"10.1101\/cshperspect.a021642","article-title":"Type III Intermediate filaments desmin, glial fibrillary acidic protein (GFAP), vimentin, and peripherin","volume":"9","author":"Hol","year":"2017","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1111\/j.1600-0854.2004.00210.x","article-title":"Annexin-actin interactions","volume":"5","author":"Hayes","year":"2004","journal-title":"Traffic"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"8065","DOI":"10.1074\/jbc.RA117.000490","article-title":"Annexins A2 and A6 interact with the extreme N terminus of tau and thereby contribute to tau\u2019s axonal localization","volume":"293","author":"Sundermann","year":"2018","journal-title":"J. Biol. Chem."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"6123","DOI":"10.1128\/JVI.07016-11","article-title":"Ultrastructural visualization of individual tegument protein dissociation during entry of herpes simplex virus 1 into human and rat dorsal root ganglion neurons","volume":"86","author":"Aggarwal","year":"2012","journal-title":"J. Virol."},{"key":"ref_60","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_61","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_62","doi-asserted-by":"crossref","first-page":"1458","DOI":"10.1111\/j.1600-0854.2008.00782.x","article-title":"Two viral kinases are required for sustained long distance axon transport of a neuroinvasive herpesvirus","volume":"9","author":"Coller","year":"2008","journal-title":"Traffic"},{"key":"ref_63","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_64","doi-asserted-by":"crossref","first-page":"2795","DOI":"10.1091\/mbc.01-07-0348","article-title":"Function of dynein and dynactin in herpes simplex virus capsid transport","volume":"13","author":"Dohner","year":"2002","journal-title":"Mol. Biol. Cell"},{"key":"ref_65","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_66","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1111\/tra.12475","article-title":"Regulation of dynein-dynactin-driven vesicular transport","volume":"18","author":"Liu","year":"2017","journal-title":"Traffic"},{"key":"ref_67","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_68","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_69","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_70","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_71","doi-asserted-by":"crossref","first-page":"382","DOI":"10.1038\/s41580-018-0004-3","article-title":"The cytoplasmic dynein transport machinery and its many cargoes","volume":"19","author":"Redwine","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_72","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_73","doi-asserted-by":"crossref","first-page":"e00538\u201317","DOI":"10.1128\/JVI.00538-17","article-title":"Microtubule Regulation and Function during Virus Infection","volume":"91","author":"Naghavi","year":"2017","journal-title":"J. Virol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.ceb.2010.08.008","article-title":"Microtubule tip-interacting proteins: A view from both ends","volume":"23","author":"Jiang","year":"2011","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.devcel.2006.05.012","article-title":"CLASPs attach microtubule plus ends to the cell cortex through a complex with LL5beta","volume":"11","author":"Lansbergen","year":"2006","journal-title":"Dev. Cell"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"13190","DOI":"10.1523\/JNEUROSCI.0935-13.2013","article-title":"Ordered recruitment of dynactin to the microtubule plus-end is required for efficient initiation of retrograde axonal transport","volume":"33","author":"Moughamian","year":"2013","journal-title":"J. Neurosci."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"12818","DOI":"10.1073\/pnas.1512559112","article-title":"Dynamic ubiquitination drives herpesvirus neuroinvasion","volume":"112","author":"Huffmaster","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1016\/j.molcel.2005.07.003","article-title":"A deubiquitinating enzyme encoded by HSV-1 belongs to a family of cysteine proteases that is conserved across the family Herpesviridae","volume":"19","author":"Kattenhorn","year":"2005","journal-title":"Mol. Cell"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"15582","DOI":"10.1128\/JVI.79.24.15582-15585.2005","article-title":"A deubiquitinating activity is conserved in the large tegument protein of the herpesviridae","volume":"79","author":"Schlieker","year":"2005","journal-title":"J. Virol."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1016\/j.molcel.2007.01.033","article-title":"Structure of a herpesvirus-encoded cysteine protease reveals a unique class of deubiquitinating enzymes","volume":"25","author":"Schlieker","year":"2007","journal-title":"Mol. Cell"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"3389","DOI":"10.1128\/JVI.02090-08","article-title":"Translocation of incoming pseudorabies virus capsids to the cell nucleus is delayed in the absence of tegument protein pUL37","volume":"83","author":"Krautwald","year":"2009","journal-title":"J. Virol."},{"key":"ref_82","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.A. (2017). The pUL37 tegument protein guides alpha-herpesvirus retrograde axonal transport to promote neuroinvasion. PLoS Pathog., 13.","DOI":"10.1371\/journal.ppat.1006741"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/B978-0-12-405210-9.00003-5","article-title":"Cellular and molecular biology of neuronal dystonin","volume":"300","author":"Ferrier","year":"2013","journal-title":"Int Rev. Cell Mol. Biol."},{"key":"ref_84","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_85","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1083\/jcb.201107096","article-title":"Microtubule stability, Golgi organization, and transport flux require dystonin-a2-MAP1B interaction","volume":"196","author":"Ryan","year":"2012","journal-title":"J. Cell Biol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1083\/jcb.200306075","article-title":"BPAG1n4 is essential for retrograde axonal transport in sensory neurons","volume":"163","author":"Liu","year":"2003","journal-title":"J. Cell Biol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"2223","DOI":"10.1073\/pnas.0602222104","article-title":"Retrolinkin, a membrane protein, plays an important role in retrograde axonal transport","volume":"104","author":"Liu","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_88","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_89","doi-asserted-by":"crossref","first-page":"770","DOI":"10.1016\/j.chom.2016.10.011","article-title":"A Viral deamidase targets the helicase domain of RIG-I to block RNA-induced activation","volume":"20","author":"Zhao","year":"2016","journal-title":"Cell Host Microbe"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1016\/j.chom.2018.07.004","article-title":"Species-specific deamidation of cGAS by herpes simplex virus UL37 protein facilitates viral replication","volume":"24","author":"Zhang","year":"2018","journal-title":"Cell Host Microbe"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"e01172-19","DOI":"10.1128\/JVI.01172-19","article-title":"The herpes simplex virus type I deamidase enhances propagation but is dispensable for retrograde axonal transport into the nervous system","volume":"93","author":"Stults","year":"2019","journal-title":"J. Virol."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"4922","DOI":"10.1128\/MCB.20.13.4922-4931.2000","article-title":"Herpes simplex virus type 1 entry into host cells: Reconstitution of capsid binding and uncoating at the nuclear pore complex in vitro","volume":"20","author":"Ojala","year":"2000","journal-title":"Mol. Cell. Biol."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"1660","DOI":"10.1128\/JVI.01139-08","article-title":"Herpes simplex virus replication: Roles of viral proteins and nucleoporins in capsid-nucleus attachment","volume":"83","author":"Copeland","year":"2009","journal-title":"J. Virol."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"8998","DOI":"10.1128\/JVI.01209-12","article-title":"A Nuclear localization signal in herpesvirus protein VP1-2 is essential for infection via capsid routing to the nuclear pore","volume":"86","author":"Abaitua","year":"2012","journal-title":"J. Virol."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"3682","DOI":"10.1128\/JVI.06432-11","article-title":"The C terminus of the large tegument protein pUL36 contains multiple capsid binding sites that function differently during assembly and cell entry of herpes simplex virus","volume":"86","author":"Schipke","year":"2012","journal-title":"J. Virol."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"2024","DOI":"10.1128\/JVI.01895-10","article-title":"A single mutation responsible for temperature-sensitive entry and assembly defects in the VP1-2 protein of herpes simplex virus","volume":"85","author":"Abaitua","year":"2011","journal-title":"J. Virol."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"3311","DOI":"10.1128\/JVI.01919-07","article-title":"Proteolytic cleavage of VP1-2 is required for release of herpes simplex virus 1 DNA into the nucleus","volume":"82","author":"Jovasevic","year":"2008","journal-title":"J. Virol."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"eaao7298","DOI":"10.1126\/science.aao7298","article-title":"Structure of the herpes simplex virus 1 capsid with associated tegument protein complexes","volume":"360","author":"Dai","year":"2018","journal-title":"Science"},{"key":"ref_99","doi-asserted-by":"crossref","unstructured":"Mettenleiter, T.C. (2016). Vesicular nucleo-cytoplasmic transport-herpesviruses as pioneers in cell biology. Viruses, 8.","DOI":"10.3390\/v8100266"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/bs.aivir.2016.07.002","article-title":"Have nec coat, will travel: Structural basis of membrane budding during nuclear egress in herpesviruses","volume":"97","author":"Bigalke","year":"2017","journal-title":"Adv. Virus Res."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1146\/annurev-virology-110615-042215","article-title":"Nuclear exodus: Herpesviruses lead the way","volume":"3","author":"Bigalke","year":"2016","journal-title":"Annu. Rev. Virol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"3379","DOI":"10.1038\/s41467-018-05889-9","article-title":"ESCRT-III mediates budding across the inner nuclear membrane and regulates its integrity","volume":"9","author":"Arii","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s40588-019-0112-7","article-title":"Beyond the NEC: Modulation of herpes simplex virus nuclear egress by viral and cellular components","volume":"6","author":"Banfield","year":"2019","journal-title":"Curr. Clin. Microbiol. Rep."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"316","DOI":"10.1016\/j.virol.2006.11.031","article-title":"Herpes simplex virus type 1 tegument proteins VP1\/2 and UL37 are associated with intranuclear capsids","volume":"361","author":"Bucks","year":"2007","journal-title":"Virology"},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"9641","DOI":"10.1128\/JVI.01045-09","article-title":"Intracellular localization of the pseudorabies virus large tegument protein pUL36","volume":"83","author":"Mohl","year":"2009","journal-title":"J. Virol."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"6303","DOI":"10.1128\/JVI.07051-11","article-title":"Nuclear egress of pseudorabies virus capsids is enhanced by a subspecies of the large tegument protein that is lost upon cytoplasmic maturation","volume":"86","author":"Leelawong","year":"2012","journal-title":"J. Virol."},{"key":"ref_107","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_108","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_109","doi-asserted-by":"crossref","first-page":"4264","DOI":"10.1128\/JVI.80.9.4264-4275.2006","article-title":"Reconstitution of herpes simplex virus microtubule-dependent trafficking in vitro","volume":"80","author":"Lee","year":"2006","journal-title":"J. Virol."},{"key":"ref_110","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_111","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_112","doi-asserted-by":"crossref","first-page":"6448","DOI":"10.1128\/JVI.72.8.6448-6455.1998","article-title":"Herpes simplex virus type 1 tegument protein VP22 induces the stabilization and hyperacetylation of microtubules","volume":"72","author":"Elliott","year":"1998","journal-title":"J. Virol."},{"key":"ref_113","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_114","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_115","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_116","doi-asserted-by":"crossref","unstructured":"Wloga, D., Joachimiak, E., and Fabczak, H. (2017). Tubulin post-translational modifications and microtubule dynamics. Int. J. Mol. Sci., 18.","DOI":"10.3390\/ijms18102207"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"2166","DOI":"10.1016\/j.cub.2006.09.014","article-title":"Microtubule acetylation promotes kinesin-1 binding and transport","volume":"16","author":"Reed","year":"2006","journal-title":"Curr. Biol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"4204","DOI":"10.1038\/emboj.2012.262","article-title":"Endocytic tubules regulated by Rab GTPases 5 and 11 are used for envelopment of herpes simplex virus","volume":"31","author":"Hollinshead","year":"2012","journal-title":"EMBO J."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1111\/tra.12134","article-title":"Rab6 dependent post-Golgi trafficking of HSV1 envelope proteins to sites of virus envelopment","volume":"15","author":"Johns","year":"2014","journal-title":"Traffic"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"8847","DOI":"10.1128\/JVI.79.14.8847-8860.2005","article-title":"Herpes simplex virus type 1 capsids transit by the trans-Golgi network, where viral glycoproteins accumulate independently of capsid egress","volume":"79","author":"Turcotte","year":"2005","journal-title":"J. Virol."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"1236","DOI":"10.1128\/JVI.75.3.1236-1251.2001","article-title":"Characterization of herpes simplex virus-containing organelles by subcellular fractionation: Role for organelle acidification in assembly of infectious particles","volume":"75","author":"Harley","year":"2001","journal-title":"J. Virol."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"3675","DOI":"10.1128\/JVI.75.8.3675-3684.2001","article-title":"Egress of alphaherpesviruses: Comparative ultrastructural study","volume":"75","author":"Granzow","year":"2001","journal-title":"J. Virol."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"1443","DOI":"10.1111\/j.1600-0854.2012.01399.x","article-title":"Herpesviruses exploit several host compartments for envelopment","volume":"13","author":"Henaff","year":"2012","journal-title":"Traffic"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"3047","DOI":"10.1007\/s00018-004-4269-7","article-title":"The role of the trans-Golgi network in varicella zoster virus biology","volume":"61","author":"Hambleton","year":"2004","journal-title":"Cell Mol. Life Sci."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"9934","DOI":"10.1128\/JVI.76.19.9934-9951.2002","article-title":"In rat dorsal root ganglion neurons, herpes simplex virus type 1 tegument forms in the cytoplasm of the cell body","volume":"76","author":"Boadle","year":"2002","journal-title":"J. Virol."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"4895","DOI":"10.1128\/JVI.03292-12","article-title":"Analysis of the early steps of herpes simplex virus 1 capsid tegumentation","volume":"87","author":"Henaff","year":"2013","journal-title":"J. Virol."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"11879","DOI":"10.1128\/JVI.78.21.11879-11889.2004","article-title":"Essential function of the pseudorabies virus UL36 gene product is independent of its interaction with the UL37 protein","volume":"78","author":"Fuchs","year":"2004","journal-title":"J. Virol."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"8927","DOI":"10.1128\/JVI.75.19.8927-8936.2001","article-title":"Pseudorabies virus UL37 gene product is involved in secondary envelopment","volume":"75","author":"Klupp","year":"2001","journal-title":"J. Virol."},{"key":"ref_129","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_130","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_131","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_132","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_133","doi-asserted-by":"crossref","first-page":"11372","DOI":"10.1128\/JVI.01893-15","article-title":"Herpes simplex virus capsid-organelle association in the absence of the large tegument protein UL36p","volume":"89","author":"Kharkwal","year":"2015","journal-title":"J. Virol."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"7257","DOI":"10.1128\/JVI.00857-16","article-title":"HSV capsid localization to ESCRT-VPS4 complexes in the presence and absence of the large tegument protein UL36p","volume":"90","author":"Kharkwal","year":"2016","journal-title":"J. Virol."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"5927","DOI":"10.1128\/JVI.00278-14","article-title":"Herpes simplex virus 1 protein UL37 interacts with viral glycoprotein gK and membrane protein UL20 and functions in cytoplasmic virion envelopment","volume":"88","author":"Jambunathan","year":"2014","journal-title":"J. Virol."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"10351","DOI":"10.1128\/JVI.01202-16","article-title":"Herpes Simplex Virus 1 UL37 Protein Tyrosine Residues Conserved among All Alphaherpesviruses Are Required for Interactions with Glycoprotein K, Cytoplasmic Virion Envelopment, and Infectious Virus Production","volume":"90","author":"Chouljenko","year":"2016","journal-title":"J. Virol."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"7380","DOI":"10.1128\/JVI.00222-07","article-title":"Herpes simplex virus type 1 cytoplasmic envelopment requires functional Vps4","volume":"81","author":"Crump","year":"2007","journal-title":"J. Virol."},{"key":"ref_138","doi-asserted-by":"crossref","unstructured":"Ibiricu, I., Huiskonen, J.T., Dohner, K., Bradke, F., Sodeik, B., and Grunewald, K. (2011). Cryo electron tomography of herpes simplex virus during axonal transport and secondary envelopment in primary neurons. PLoS Pathog., 7.","DOI":"10.1371\/journal.ppat.1002406"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"6152","DOI":"10.1073\/pnas.1817924116","article-title":"Intracellular cargo transport by single-headed kinesin motors","volume":"116","author":"Schimert","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_140","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_141","doi-asserted-by":"crossref","first-page":"1089","DOI":"10.1152\/physrev.00023.2007","article-title":"Intracellular transport and kinesin superfamily proteins, KIFs: Structure, function, and dynamics","volume":"88","author":"Hirokawa","year":"2008","journal-title":"Physiol. Rev."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"14467","DOI":"10.1128\/JVI.02777-14","article-title":"Blocking ESCRT-mediated envelopment inhibits microtubule-dependent trafficking of alphaherpesviruses in vitro","volume":"88","author":"Kharkwal","year":"2014","journal-title":"J. Virol."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1146\/annurev-cellbio-100616-060600","article-title":"Structures, functions, and dynamics of ESCRT-III\/Vps4 membrane remodeling and fission complexes","volume":"34","author":"McCullough","year":"2018","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"1548","DOI":"10.1126\/science.aad8305","article-title":"Structure and membrane remodeling activity of ESCRT-III helical polymers","volume":"350","author":"McCullough","year":"2015","journal-title":"Science"},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1016\/j.tibs.2016.08.016","article-title":"Cellular functions and molecular mechanisms of the ESCRT membrane-scission machinery","volume":"42","author":"Christ","year":"2017","journal-title":"Trends Biochem. Sci."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1002\/rmv.1724","article-title":"Making the case: Married versus separate models of alphaherpes virus anterograde transport in axons","volume":"22","author":"Kratchmarov","year":"2012","journal-title":"Rev. Med. Virol."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"414","DOI":"10.1002\/rmv.1760","article-title":"Letter in response to: Making the case: Married versus separate models of alphaherpes virus anterograde transport in axons","volume":"23","author":"Cunningham","year":"2013","journal-title":"Rev. Med. Virol."},{"key":"ref_148","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_149","doi-asserted-by":"crossref","first-page":"9997","DOI":"10.1128\/JVI.01122-16","article-title":"Dual-color herpesvirus capsids discriminate inoculum from progeny and reveal axonal transport dynamics","volume":"90","author":"Scherer","year":"2016","journal-title":"J. Virol."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/j.virol.2010.10.009","article-title":"Completely assembled virus particles detected by transmission electron microscopy in proximal and mid-axons of neurons infected with herpes simplex virus type 1, herpes simplex virus type 2 and pseudorabies virus","volume":"409","author":"Huang","year":"2011","journal-title":"Virology"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"3592","DOI":"10.1128\/JVI.80.7.3592-3606.2006","article-title":"Herpes simplex virus type 1 accumulation, envelopment, and exit in growth cones and varicosities in mid-distal regions of axons","volume":"80","author":"Wakisaka","year":"2006","journal-title":"J. Virol."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"3187","DOI":"10.1128\/JVI.01579-08","article-title":"Herpes simplex virus utilizes the large secretory vesicle pathway for anterograde transport of tegument and envelope proteins and for viral exocytosis from growth cones of human fetal axons","volume":"83","author":"Boadle","year":"2009","journal-title":"J. Virol."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"6529","DOI":"10.1073\/pnas.91.14.6529","article-title":"Axonal transport of herpes simplex virions to epidermal cells: Evidence for a specialized mode of virus transport and assembly","volume":"91","author":"Penfold","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"11165","DOI":"10.1128\/JVI.01107-06","article-title":"Herpes simplex virus capsids are transported in neuronal axons without an envelope containing the viral glycoproteins","volume":"80","author":"Snyder","year":"2006","journal-title":"J. Virol."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"8337","DOI":"10.1128\/JVI.00520-07","article-title":"A herpes simplex virus gD-YFP fusion glycoprotein is transported separately from viral capsids in neuronal axons","volume":"81","author":"Snyder","year":"2007","journal-title":"J. Virol."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"974","DOI":"10.1016\/j.neuroscience.2007.02.010","article-title":"Viral regulation of the long distance axonal transport of herpes simplex virus nucleocapsid","volume":"146","author":"LaVail","year":"2007","journal-title":"Neuroscience"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"1217","DOI":"10.1523\/JNEUROSCI.17-04-01217.1997","article-title":"Characterization of a CNS cell line, CAD, in which morphological differentiation is initiated by serum deprivation","volume":"17","author":"Qi","year":"1997","journal-title":"J. Neurosci."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"2601","DOI":"10.1002\/jnr.21216","article-title":"Studies of the central nervous system-derived CAD cell line, a suitable model for intraneuronal transport studies?","volume":"85","author":"Li","year":"2007","journal-title":"J. Neurosci. Res."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"13019","DOI":"10.1128\/JVI.01296-10","article-title":"Resolving the assembly state of herpes simplex virus during axon transport by live-cell imaging","volume":"84","author":"Antinone","year":"2010","journal-title":"J. Virol."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"13031","DOI":"10.1128\/JVI.01784-10","article-title":"Ultrastructural analysis of virion formation and intraaxonal transport of herpes simplex virus type 1 in primary rat neurons","volume":"84","author":"Negatsch","year":"2010","journal-title":"J. Virol."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"e00050\u201317","DOI":"10.1128\/JVI.00050-17","article-title":"Herpes simplex virus gE\/gI and US9 promote both envelopment and sorting of virus particles in the cytoplasm of neurons, two processes that precede anterograde transport in axons","volume":"91","author":"DuRaine","year":"2017","journal-title":"J. Virol."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"5919","DOI":"10.1128\/JVI.00116-11","article-title":"Anterograde transport of herpes simplex virus capsids in neurons by both separate and married mechanisms","volume":"85","author":"Wisner","year":"2011","journal-title":"J. Virol."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"8503","DOI":"10.1128\/JVI.73.10.8503-8511.1999","article-title":"Anterograde transport of herpes simplex virus proteins in axons of peripheral human fetal neurons: An immunoelectron microscopy study","volume":"73","author":"Holland","year":"1999","journal-title":"J. Virol."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1016\/j.neulet.2011.01.018","article-title":"KIF1A is the primary anterograde motor protein required for the axonal transport of dense-core vesicles in cultured hippocampal neurons","volume":"491","author":"Lo","year":"2011","journal-title":"Neurosci. Lett."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1099\/0022-1317-72-3-661","article-title":"Identification and characterization of a novel non-infectious herpes simplex virus-related particle","volume":"72","author":"Szilagyi","year":"1991","journal-title":"J. Gen. Virol."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"2565","DOI":"10.3389\/fmicb.2017.02565","article-title":"Role of L-particles during herpes simplex virus infection","volume":"8","author":"Heilingloh","year":"2017","journal-title":"Front. Microbiol."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1099\/0022-1317-73-2-277","article-title":"Assembly of enveloped tegument structures (L particles) can occur independently of virion maturation in herpes simplex virus type 1-infected cells","volume":"73","author":"Rixon","year":"1992","journal-title":"J. Gen. Virol."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1099\/0022-1317-73-2-269","article-title":"Characterization of enveloped tegument structures (L particles) produced by alphaherpesviruses: Integrity of the tegument does not depend on the presence of capsid or envelope","volume":"73","author":"McLauchlan","year":"1992","journal-title":"J. Gen. Virol."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"e01259\u201318","DOI":"10.1128\/JVI.01259-18","article-title":"Qualitative differences in capsidless L-particles released as a by-product of bovine herpesvirus 1 and herpes simplex virus 1 infections","volume":"92","author":"Russell","year":"2018","journal-title":"J. Virol."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"e00063-12","DOI":"10.1128\/mBio.00063-12","article-title":"Visualization of an alphaherpesvirus membrane protein that is essential for anterograde axonal spread of infection in neurons","volume":"3","author":"Taylor","year":"2012","journal-title":"MBio"},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"5657","DOI":"10.1128\/JVI.77.10.5657-5667.2003","article-title":"L-particle production during primary replication of pseudorabies virus in the nasal mucosa of swine","volume":"77","author":"Aleman","year":"2003","journal-title":"J. Virol."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"6511","DOI":"10.1128\/JVI.00625-15","article-title":"Us9-independent axonal sorting and transport of the pseudorabies virus glycoprotein gM","volume":"89","author":"Kratchmarov","year":"2015","journal-title":"J. Virol."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1111\/cmi.12093","article-title":"Characterization of herpes simplex virus type 1 L-particle assembly and egress in hippocampal neurones by electron cryo-tomography","volume":"15","author":"Ibiricu","year":"2013","journal-title":"Cell. Microbiol."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1016\/S0065-3527(08)60787-3","article-title":"Infection and spread of alphaherpesviruses in the nervous system","volume":"51","author":"Enquist","year":"1998","journal-title":"Adv. Virus Res."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"10975","DOI":"10.1128\/JVI.74.23.10975-10983.2000","article-title":"Pseudorabies virus membrane proteins gI and gE facilitate anterograde spread of infection in projection-specific neurons in the rat","volume":"74","author":"Husak","year":"2000","journal-title":"J. Virol."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"6455","DOI":"10.1128\/jvi.71.9.6455-6464.1997","article-title":"Characterization of pseudorabies virus mutants expressing carboxy-terminal truncations of gE: Evidence for envelope incorporation, virulence, and neurotropism domains","volume":"71","author":"Tirabassi","year":"1997","journal-title":"J. Virol."},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"8835","DOI":"10.1128\/JVI.79.14.8835-8846.2005","article-title":"Efficient axonal localization of alphaherpesvirus structural proteins in cultured sympathetic neurons requires viral glycoprotein E","volume":"79","author":"Enquist","year":"2005","journal-title":"J. Virol."},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1128\/JVI.74.2.834-845.2000","article-title":"Role of pseudorabies virus Us9, a type II membrane protein, in infection of tissue culture cells and the rat nervous system","volume":"74","author":"Brideau","year":"2000","journal-title":"J. Virol."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"6978","DOI":"10.1128\/JVI.00598-09","article-title":"Comparison of the pseudorabies virus Us9 protein with homologs from other veterinary and human alphaherpesviruses","volume":"83","author":"Lyman","year":"2009","journal-title":"J. Virol."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"4560","DOI":"10.1128\/JVI.72.6.4560-4570.1998","article-title":"The Us9 gene product of pseudorabies virus, an alphaherpesvirus, is a phosphorylated, tail-anchored type II membrane protein","volume":"72","author":"Brideau","year":"1998","journal-title":"J. Virol."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"4549","DOI":"10.1128\/JVI.74.10.4549-4561.2000","article-title":"Directional transneuronal infection by pseudorabies virus is dependent on an acidic internalization motif in the Us9 cytoplasmic tail","volume":"74","author":"Brideau","year":"2000","journal-title":"J. Virol."},{"key":"ref_182","doi-asserted-by":"crossref","unstructured":"Lyman, M.G., Curanovic, D., and Enquist, L.W. (2008). Targeting of pseudorabies virus structural proteins to axons requires association of the viral Us9 protein with lipid rafts. PLoS Pathog., 4.","DOI":"10.1371\/journal.ppat.1000065"},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"821","DOI":"10.1128\/JVI.75.2.821-833.2001","article-title":"Herpes simplex virus gE\/gI sorts nascent virions to epithelial cell junctions, promoting virus spread","volume":"75","author":"Johnson","year":"2001","journal-title":"J. Virol."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"7087","DOI":"10.1128\/jvi.69.11.7087-7098.1995","article-title":"Glycoproteins E and I facilitate neuron-to-neuron spread of herpes simplex virus","volume":"69","author":"Dingwell","year":"1995","journal-title":"J. Virol."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/j.virol.2010.06.006","article-title":"Herpes simplex virus type 2 glycoprotein E is required for efficient virus spread from epithelial cells to neurons and for targeting viral proteins from the neuron cell body into axons","volume":"405","author":"Wang","year":"2010","journal-title":"Virology"},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"11462","DOI":"10.1073\/pnas.0503230102","article-title":"Herpes keratitis in the absence of anterograde transport of virus from sensory ganglia to the cornea","volume":"102","author":"Polcicova","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"8315","DOI":"10.1128\/JVI.00633-09","article-title":"Anterograde spread of herpes simplex virus type 1 requires glycoprotein E and glycoprotein I but not Us9","volume":"83","author":"McGraw","year":"2009","journal-title":"J. Virol."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"10613","DOI":"10.1128\/JVI.01241-08","article-title":"Herpes simplex virus gE\/gI and US9 proteins promote transport of both capsids and virion glycoproteins in neuronal axons","volume":"82","author":"Snyder","year":"2008","journal-title":"J. Virol."},{"key":"ref_189","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_190","doi-asserted-by":"crossref","first-page":"11363","DOI":"10.1128\/JVI.01281-07","article-title":"Pseudorabies virus Us9 directs axonal sorting of viral capsids","volume":"81","author":"Lyman","year":"2007","journal-title":"J. Virol."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"10875","DOI":"10.1128\/JVI.79.17.10875-10889.2005","article-title":"Neuron-to-cell spread of pseudorabies virus in a compartmented neuronal culture system","volume":"79","author":"Enquist","year":"2005","journal-title":"J. Virol."},{"key":"ref_192","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_193","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_194","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_195","doi-asserted-by":"crossref","first-page":"2135","DOI":"10.1523\/JNEUROSCI.1922-17.2018","article-title":"The Axon Initial Segment: An Updated Viewpoint","volume":"38","author":"Leterrier","year":"2018","journal-title":"J. Neurosci"},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"1148","DOI":"10.1016\/j.cell.2009.01.016","article-title":"A selective filter for cytoplasmic transport at the axon initial segment","volume":"136","author":"Song","year":"2009","journal-title":"Cell"},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"e01269-18","DOI":"10.1128\/JVI.01269-18","article-title":"Kinesin-1 Proteins KIF5A, -5B, and -5C promote anterograde transport of herpes simplex virus enveloped virions in axons","volume":"92","author":"DuRaine","year":"2018","journal-title":"J. Virol."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1046\/j.1474-9728.2003.00069.x","article-title":"Fast anterograde transport of herpes simplex virus: Role for the amyloid precursor protein of alzheimer\u2019s disease","volume":"2","author":"DeGiorgis","year":"2003","journal-title":"Aging Cell"},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1016\/S1471-4914(02)02320-1","article-title":"APP on the move","volume":"8","author":"Muller","year":"2002","journal-title":"Trends Mol. Med."},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"2386","DOI":"10.1523\/JNEUROSCI.3089-04.2005","article-title":"Axonal transport, amyloid precursor protein, kinesin-1, and the processing apparatus: Revisited","volume":"25","author":"Lazarov","year":"2005","journal-title":"J. Neurosci."},{"key":"ref_201","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_202","doi-asserted-by":"crossref","first-page":"2653","DOI":"10.1128\/JVI.03023-15","article-title":"Dual role of herpes simplex virus 1 pUS9 in virus anterograde axonal transport and final assembly in growth cones in distal axons","volume":"90","author":"Boadle","year":"2016","journal-title":"J. Virol."},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"7139","DOI":"10.1523\/JNEUROSCI.1821-06.2006","article-title":"mRNA transport in dendrites: RNA granules, motors, and tracks","volume":"26","author":"Hirokawa","year":"2006","journal-title":"J. Neurosci."},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"1045","DOI":"10.1083\/jcb.200302175","article-title":"Microtubules provide directional cues for polarized axonal transport through interaction with kinesin motor head","volume":"162","author":"Nakata","year":"2003","journal-title":"J. Cell Biol."},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"11215","DOI":"10.1128\/JVI.74.23.11215-11221.2000","article-title":"Inhibition of PKR activation by the proline-rich RNA binding domain of the herpes simplex virus type 1 Us11 protein","volume":"74","author":"Poppers","year":"2000","journal-title":"J. Virol."},{"key":"ref_206","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_207","doi-asserted-by":"crossref","first-page":"9192","DOI":"10.1128\/JVI.77.17.9192-9203.2003","article-title":"Association of the herpes simplex virus type 1 Us11 gene product with the cellular kinesin light-chain-related protein PAT1 results in the redistribution of both polypeptides","volume":"77","author":"Benboudjema","year":"2003","journal-title":"J. Virol."},{"key":"ref_208","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_209","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1186\/1743-422X-6-168","article-title":"Herpes simplex virus type 2 tegument protein UL56 relocalizes ubiquitin ligase Nedd4 and has a role in transport and\/or release of virions","volume":"6","author":"Ushijima","year":"2009","journal-title":"Virol. J."},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/0168-1702(96)80248-6","article-title":"Restitution of the UL56 gene expression of HSV-1 HFEM led to restoration of virulent phenotype; deletion of the amino acids 217 to 234 of the UL56 protein abrogates the virulent phenotype","volume":"40","author":"Kehm","year":"1996","journal-title":"Virus Res."},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"6646","DOI":"10.1128\/JVI.00214-15","article-title":"Herpes Simplex Virus 1 US3 Phosphorylates Cellular KIF3A To Downregulate CD1d Expression","volume":"89","author":"Xiong","year":"2015","journal-title":"J. Virol."},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"e00820\u201316","DOI":"10.1128\/mBio.00820-16","article-title":"Exocytosis of alphaherpesvirus virions, light particles, and glycoproteins uses constitutive secretory mechanisms","volume":"7","author":"Hogue","year":"2016","journal-title":"MBio"},{"key":"ref_213","doi-asserted-by":"crossref","unstructured":"Hogue, I.B., Bosse, J.B., Hu, J.R., Thiberge, S.Y., and Enquist, L.W. (2014). Cellular mechanisms of alpha herpesvirus egress: Live cell fluorescence microscopy of pseudorabies virus exocytosis. PLoS Pathog., 10.","DOI":"10.1371\/journal.ppat.1004535"},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"17046","DOI":"10.1073\/pnas.1212926109","article-title":"Alphaherpesvirus axon-to-cell spread involves limited virion transmission","volume":"109","author":"Taylor","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"}],"container-title":["Viruses"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1999-4915\/11\/12\/1165\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T13:42:56Z","timestamp":1760190176000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1999-4915\/11\/12\/1165"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,12,17]]},"references-count":214,"journal-issue":{"issue":"12","published-online":{"date-parts":[[2019,12]]}},"alternative-id":["v11121165"],"URL":"https:\/\/doi.org\/10.3390\/v11121165","relation":{},"ISSN":["1999-4915"],"issn-type":[{"value":"1999-4915","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,12,17]]}}}