{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T00:26:18Z","timestamp":1791246378692,"version":"4.1.0"},"reference-count":122,"publisher":"MDPI AG","issue":"13","license":[{"start":{"date-parts":[[2026,6,24]],"date-time":"2026-06-24T00:00:00Z","timestamp":1782259200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100006769","name":"Russian Science Foundation","doi-asserted-by":"crossref","award":["23-64-00002"],"award-info":[{"award-number":["23-64-00002"]}],"id":[{"id":"10.13039\/501100006769","id-type":"DOI","asserted-by":"crossref"}]},{"award":["23-64-00002"],"award-info":[{"award-number":["23-64-00002"]}],"id":[{"id":"https:\/\/ror.org\/03y2gwe85","id-type":"ROR","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003443","name":"Ministry of Education and Science of the Russian Federation","doi-asserted-by":"crossref","award":["FSMG-2025-0064"],"award-info":[{"award-number":["FSMG-2025-0064"]}],"id":[{"id":"10.13039\/501100003443","id-type":"DOI","asserted-by":"crossref"}]},{"award":["FSMG-2025-0064"],"award-info":[{"award-number":["FSMG-2025-0064"]}],"id":[{"id":"https:\/\/ror.org\/00ghqgy32","id-type":"ROR","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Animal infectious diseases impose severe economic burdens on livestock industries, threaten wildlife populations, and compromise food security. Although vaccination remains the cornerstone of disease prevention, conventional vaccine platforms are often constrained by safety, efficacy, or manufacturing scalability. This narrative review provides a comprehensive analysis of the state of the art in herpesvirus-vectored vaccines for veterinary applications, focusing on five well-characterized alphaherpesviruses: Bovine herpesvirus type 1 (BoHV-1), Pseudorabies virus (PRV), Marek\u2019s disease virus (MDV), Equine herpesvirus type 1 (EHV-1), and Duck enteritis virus (DEV). The intrinsic characteristics of herpesviruses, including large, stable genomes; the capacity for foreign gene insertion; broad host tropism; and the ability to elicit robust humoral and cellular immunity, are examined, and their performance is compared with that of traditional vaccine platforms. Key advances in vectored vaccine development are highlighted, from proof-of-concept studies to the creation of advanced multivalent constructs. These approaches demonstrate protective efficacy against a range of significant animal pathogens, including foot-and-mouth disease virus, porcine reproductive and respiratory syndrome virus, avian influenza virus, infectious bursal disease virus, and West Nile virus. The literature was identified through systematic searches of PubMed, Google Scholar, and Web of Science (1990\u20132026), followed by title\/abstract screening and reference chaining. Future directions in vector engineering, mucosal delivery, and synthetic biology approaches are considered. Herpesvirus-vectored vaccines represent a versatile platform for enhancing animal health, supporting sustainable agriculture, and mitigating zoonotic risks.<\/jats:p>","DOI":"10.3390\/ijms27135686","type":"journal-article","created":{"date-parts":[[2026,6,25]],"date-time":"2026-06-25T05:48:16Z","timestamp":1782366496000},"page":"5686","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Recombinant Alphaherpesvirus Vectors in Veterinary Vaccinology: Platforms, Applications, and Translational Challenges"],"prefix":"10.3390","volume":"27","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5982-8393","authenticated-orcid":false,"given":"Ali","family":"Mazloum","sequence":"first","affiliation":[{"name":"Moscow Center for Advanced Studies, Kulakova Street 20, Moscow 123592, Russia"},{"name":"Federal Research Center for Innovator and Emerging Biomedical and Pharmaceutical Technologies, Moscow 125315, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7608-439X","authenticated-orcid":false,"given":"Sofya G.","family":"Feoktistova","sequence":"additional","affiliation":[{"name":"Moscow Center for Advanced Studies, Kulakova Street 20, Moscow 123592, Russia"},{"name":"Federal Research Center for Innovator and Emerging Biomedical and Pharmaceutical Technologies, Moscow 125315, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Veronika","family":"Ledyaeva","sequence":"additional","affiliation":[{"name":"Moscow Center for Advanced Studies, Kulakova Street 20, Moscow 123592, Russia"},{"name":"Federal Research Center for Innovator and Emerging Biomedical and Pharmaceutical Technologies, Moscow 125315, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gava","family":"Khulkhachiev","sequence":"additional","affiliation":[{"name":"Federal Research Center for Innovator and Emerging Biomedical and Pharmaceutical Technologies, Moscow 125315, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9252-1601","authenticated-orcid":false,"given":"Olga N.","family":"Mityaeva","sequence":"additional","affiliation":[{"name":"Moscow Center for Advanced Studies, Kulakova Street 20, Moscow 123592, Russia"},{"name":"Federal Research Center for Innovator and Emerging Biomedical and Pharmaceutical Technologies, Moscow 125315, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pavel Yu","family":"Volchkov","sequence":"additional","affiliation":[{"name":"Moscow Center for Advanced Studies, Kulakova Street 20, Moscow 123592, Russia"},{"name":"Federal Research Center for Innovator and Emerging Biomedical and Pharmaceutical Technologies, Moscow 125315, Russia"},{"name":"Moscow Clinical Scientific Center N.A. A.S. Loginov, Novogireevskaya Street, Moscow 111123, Russia"},{"name":"Faculty of Fundamental Medicine, Lomonosov Moscow State University, Moscow 119991, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,6,24]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1038\/s41541-022-00503-y","article-title":"The use of viral vectors in vaccine development","volume":"7","author":"Travieso","year":"2022","journal-title":"npj Vaccines"},{"key":"ref_2","first-page":"21","article-title":"Edward Jenner and the history of smallpox and vaccination","volume":"18","author":"Riedel","year":"2005","journal-title":"Proc. (Bayl. Univ. Med. Cent.)"},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Sanders, B., Koldijk, M., and Schuitemaker, H. (2015). Inactivated Viral Vaccines. Vaccine Analysis: Strategies, Principles, and Control, Springer.","DOI":"10.1007\/978-3-662-45024-6_2"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1586\/erv.12.38","article-title":"Inactivated virus vaccines from chemistry to prophylaxis: Merits, risks and challenges","volume":"11","author":"Delrue","year":"2012","journal-title":"Expert Rev. Vaccines"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"e2407241","DOI":"10.1002\/advs.202407241","article-title":"Viral Live-Attenuated Vaccines (LAVs): Past and Future Directions","volume":"12","author":"Tang","year":"2025","journal-title":"Adv. Sci."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1038\/nbt.1635","article-title":"Rationalizing the development of live attenuated virus vaccines","volume":"28","author":"Lauring","year":"2010","journal-title":"Nat. Biotechnol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"18","DOI":"10.7774\/cevr.2012.1.1.18","article-title":"A review of vaccine development and research for industry animals in Korea","volume":"1","author":"Lee","year":"2012","journal-title":"Clin. Exp. Vaccine Res."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"1149","DOI":"10.1586\/erv.10.115","article-title":"Virus-like particles in vaccine development","volume":"9","author":"Mellado","year":"2010","journal-title":"Expert Rev. Vaccines"},{"key":"ref_9","doi-asserted-by":"crossref","unstructured":"Haghmorad, D., Eslami, M., Orooji, N., Halabitska, I., Kamyshna, I., and Kamyshnyi, O. (2025). mRNA vaccine platforms: Linking infectious disease prevention and cancer immunotherapy. Front. Bioeng. Biotechnol., 13.","DOI":"10.3389\/fbioe.2025.1547025"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1038\/nrd.2017.243","article-title":"mRNA vaccines\u2014A new era in vaccinology","volume":"17","author":"Pardi","year":"2018","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1017\/S146625230700134X","article-title":"A review of the biology of bovine herpesvirus type 1 (BHV-1), its role as a cofactor in the bovine respiratory disease complex and development of improved vaccines","volume":"8","author":"Jones","year":"2007","journal-title":"Anim. Health Res. Rev."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"e0101022","DOI":"10.1128\/jvi.01010-22","article-title":"Stress Triggers Expression of Bovine Herpesvirus 1 Infected Cell Protein 4 (bICP4) RNA during Early Stages of Reactivation from Latency in Pharyngeal Tonsil","volume":"96","author":"Toomer","year":"2022","journal-title":"J. Virol."},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Gao, W., Zhang, M., and Zhu, Z. (2025). The prevalence of pseudorabies virus in China from 2010 to 2024: A systematic review and meta-analysis. BMC Vet. Res., 21.","DOI":"10.1186\/s12917-025-04924-4"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"2044","DOI":"10.1038\/s41598-023-29210-x","article-title":"Purinergic signaling during Marek\u2019s disease in chickens","volume":"13","author":"Akbar","year":"2023","journal-title":"Sci. Rep."},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Oladunni, F.S., Horohov, D.W., and Chambers, T.M. (2019). EHV-1: A Constant Threat to the Horse Industry. Front. Microbiol., 10.","DOI":"10.3389\/fmicb.2019.02668"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"557","DOI":"10.5455\/javar.2021.h545","article-title":"Duck virus enteritis (duck plague) outbreak in an Australian black swan (Cygnus atratus) flock at safari park in Bangladesh: A case report","volume":"8","author":"Islam","year":"2021","journal-title":"J. Adv. Vet. Anim. Res."},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Gokduman, E.M., Atasoy, M.O., Goksu, A.G., Sozdutmaz, \u0130., and Munir, M. (2025). Potential of Bovine Herpesvirus Vectors for Recombinant Vaccines. Vaccines, 14.","DOI":"10.3390\/vaccines14010006"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"22766","DOI":"10.3402\/jom.v5i0.22766","article-title":"Herpesviruses: Latency and reactivation\u2014Viral strategies and host response","volume":"5","author":"Grinde","year":"2013","journal-title":"J. Oral Microbiol."},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Pavulraj, S., and Azab, W. (2023). Editorial: Herpesviruses of animals: Recent advances and updates. Front. Vet. Sci., 10.","DOI":"10.3389\/fvets.2023.1326282"},{"key":"ref_20","first-page":"1823","article-title":"Herpes Simplex Viruses","volume":"Volume 6","author":"Knipe","year":"2013","journal-title":"Fields Virology"},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Weidner-Glunde, M., Kruminis-Kaszkiel, E., and Savanagouder, M. (2020). Herpesviral Latency-Common Themes. Pathogens, 9.","DOI":"10.3390\/pathogens9020125"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1186\/2042-4280-2-3","article-title":"Tegument protein control of latent herpesvirus establishment and animation","volume":"2","author":"Penkert","year":"2011","journal-title":"Herpesviridae"},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Michalak, K.P., and Adamski, W. (2026). A System-Level Perspective on Epstein-Barr Virus Persistence: The Partial Lytic Reactivation. Int. J. Mol. Sci., 27.","DOI":"10.3390\/ijms27073337"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"102343","DOI":"10.1016\/j.xpro.2023.102343","article-title":"In vitro infection of primary chicken lymphocytes with Marek\u2019s disease virus","volume":"4","author":"Bertzbach","year":"2023","journal-title":"STAR Protoc."},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Cliffe, A., Chang, L., Colgrove, R., and Knipe, D.M. (2014). Herpes Simplex Virus. Reference Module in Biomedical Sciences, Elsevier.","DOI":"10.1016\/B978-0-12-801238-3.00080-5"},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Tien, Y.T., Akbar, H., and Jarosinski, K.W. (2023). Temperature-induced reactivation of Marek\u2019s disease virus-transformed T cells ex vivo. Front. Vet. Sci., 10.","DOI":"10.3389\/fvets.2023.1145757"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"e0148621","DOI":"10.1128\/jvi.01486-21","article-title":"Bovine Herpesvirus 1 Invasion of Sensory Neurons by Retrograde Axonal Transport Is Dependent on the pUL37 Region 2 Effector","volume":"96","author":"Stults","year":"2022","journal-title":"J. Virol."},{"key":"ref_28","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_29","doi-asserted-by":"crossref","unstructured":"Ferrara, G., Sgadari, M., Longobardi, C., Iovane, G., Pagnini, U., and Montagnaro, S. (2023). Autophagy up-regulation upon FeHV-1 infection on permissive cells. Front. Vet. Sci., 10.","DOI":"10.3389\/fvets.2023.1174681"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"1063","DOI":"10.1128\/JVI.78.3.1063-1068.2004","article-title":"Herpes simplex virus virion host shutoff protein: Immune evasion mediated by a viral RNase?","volume":"78","author":"Smiley","year":"2004","journal-title":"J. Virol."},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"Ma, H., Yin, R., and Ren, L. (Anim. Zoonoses, 2025). Recent advances on herpesvirus unique long protein 41, Anim. Zoonoses, in press.","DOI":"10.1016\/j.azn.2025.12.002"},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Dauber, B., Saffran, H.A., and Smiley, J.R. (2019). The herpes simplex virus host shutoff (vhs) RNase limits accumulation of double stranded RNA in infected cells: Evidence for accelerated decay of duplex RNA. PLoS Pathog., 15.","DOI":"10.1371\/journal.ppat.1008111"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"3366","DOI":"10.1073\/pnas.0611128104","article-title":"Host shutoff during productive Epstein-Barr virus infection is mediated by BGLF5 and may contribute to immune evasion","volume":"104","author":"Rowe","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"2385","DOI":"10.1128\/JVI.01946-07","article-title":"The DNase of gammaherpesviruses impairs recognition by virus-specific CD8+ T cells through an additional host shutoff function","volume":"82","author":"Zuo","year":"2008","journal-title":"J. Virol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1016\/j.virol.2004.01.019","article-title":"Herpes simplex virus 2 virion host shutoff protein interferes with type I interferon production and responsiveness","volume":"322","author":"Duerst","year":"2004","journal-title":"Virology"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"438","DOI":"10.3390\/cells3020438","article-title":"HSV-1 ICP0: An E3 Ubiquitin Ligase That Counteracts Host Intrinsic and Innate Immunity","volume":"3","author":"Mostafa","year":"2014","journal-title":"Cells"},{"key":"ref_37","doi-asserted-by":"crossref","unstructured":"Wang, C., Li, L., Zhai, X., Chang, H., and Liu, H. (2024). Evasion of the Antiviral Innate Immunity by PRV. Int. J. Mol. Sci., 25.","DOI":"10.3390\/ijms252313140"},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"Jones, C. (2019). Bovine Herpesvirus 1 Counteracts Immune Responses and Immune-Surveillance to Enhance Pathogenesis and Virus Transmission. Front. Immunol., 10.","DOI":"10.3389\/fimmu.2019.01008"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1831","DOI":"10.1128\/JVI.78.4.1831-1842.2004","article-title":"A cytomegalovirus inhibitor of gamma interferon signaling controls immunoproteasome induction","volume":"78","author":"Khan","year":"2004","journal-title":"J. Virol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"12616","DOI":"10.1073\/pnas.94.23.12616","article-title":"Inhibition of ubiquitin\/proteasome-dependent protein degradation by the Gly-Ala repeat domain of the Epstein-Barr virus nuclear antigen 1","volume":"94","author":"Levitskaya","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1720","DOI":"10.1038\/sj.emboj.7601058","article-title":"Glycine-alanine repeats impair proper substrate unfolding by the proteasome","volume":"25","author":"Hoyt","year":"2006","journal-title":"EMBO J."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"4894","DOI":"10.4049\/jimmunol.181.7.4894","article-title":"The varicellovirus UL49.5 protein blocks the transporter associated with antigen processing (TAP) by inhibiting essential conformational transitions in the 6+6 transmembrane TAP core complex","volume":"181","author":"Verweij","year":"2008","journal-title":"J. Immunol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"2038","DOI":"10.1016\/j.molimm.2011.06.438","article-title":"Structural and functional analysis of the TAP-inhibiting UL49.5 proteins of varicelloviruses","volume":"48","author":"Verweij","year":"2011","journal-title":"Mol. Immunol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/j.virol.2014.11.008","article-title":"An MHC class I immune evasion gene of Marek\u05f3s disease virus","volume":"475","author":"Hearn","year":"2015","journal-title":"Virology"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1093\/emboj\/20.3.387","article-title":"The human cytomegalovirus gene product US6 inhibits ATP binding by TAP","volume":"20","author":"Hewitt","year":"2001","journal-title":"EMBO J."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"3554","DOI":"10.1128\/JVI.06994-11","article-title":"Identification and Characterization of Equine Herpesvirus Type 1 pUL56 and Its Role in Virus-Induced Downregulation of Major Histocompatibility Complex Class I","volume":"86","author":"Ma","year":"2012","journal-title":"J. Virol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"12802","DOI":"10.1128\/JVI.02079-14","article-title":"Major Histocompatibility Complex Class I Downregulation Induced by Equine Herpesvirus Type 1 pUL56 Is through Dynamin-Dependent Endocytosis","volume":"88","author":"Huang","year":"2014","journal-title":"J. Virol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1038\/384432a0","article-title":"Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction","volume":"384","author":"Wiertz","year":"1996","journal-title":"Nature"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"8636","DOI":"10.1074\/jbc.M513920200","article-title":"The viral E3 ubiquitin ligase mK3 uses the Derlin\/p97 endoplasmic reticulum-associated degradation pathway to mediate down-regulation of major histocompatibility complex class I proteins","volume":"281","author":"Wang","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"9034","DOI":"10.1128\/JVI.00711-07","article-title":"Downregulation of class I major histocompatibility complex surface expression by varicella-zoster virus involves open reading frame 66 protein kinase-dependent and -independent mechanisms","volume":"81","author":"Eisfeld","year":"2007","journal-title":"J. Virol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"8852","DOI":"10.1128\/JVI.78.16.8852-8859.2004","article-title":"Internalization of pseudorabies virus glycoprotein B is mediated by an interaction between the YQRL motif in its cytoplasmic domain and the clathrin-associated AP-2 adaptor complex","volume":"78","author":"Favoreel","year":"2004","journal-title":"J. Virol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"8051","DOI":"10.1073\/pnas.140129797","article-title":"Kaposi\u2019s sarcoma-associated herpesvirus encodes two proteins that block cell surface display of MHC class I chains by enhancing their endocytosis","volume":"97","author":"Coscoy","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_53","doi-asserted-by":"crossref","unstructured":"Zuo, J., Currin, A., Griffin, B.D., Shannon-Lowe, C., Thomas, W.A., Ressing, M.E., Rickinson, A.B., and Rowe, M. (2009). The Epstein-Barr virus G-protein-coupled receptor contributes to immune evasion by targeting MHC class I molecules for degradation. PLoS Pathog., 5.","DOI":"10.1371\/journal.ppat.1000255"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"5197","DOI":"10.1128\/JVI.75.11.5197-5204.2001","article-title":"Human cytomegalovirus US2 endoplasmic reticulum-lumenal domain dictates association with major histocompatibility complex class I in a locus-specific manner","volume":"75","author":"Gewurz","year":"2001","journal-title":"J. Virol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"514","DOI":"10.1038\/386514a0","article-title":"The class I MHC homologue of human cytomegalovirus inhibits attack by natural killer cells","volume":"386","author":"Reyburn","year":"1997","journal-title":"Nature"},{"key":"ref_56","doi-asserted-by":"crossref","unstructured":"Denaeghel, S., De Pelsmaeker, S., Van Waesberghe, C., and Favoreel, H.W. (2021). Pseudorabies Virus Infection Causes Downregulation of Ligands for the Activating NK Cell Receptor NKG2D. Viruses, 13.","DOI":"10.3390\/v13020266"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"16118","DOI":"10.1073\/pnas.1409485111","article-title":"Modulation of CD112 by the alphaherpesvirus gD protein suppresses DNAM-1\u2013dependent NK cell-mediated lysis of infected cells","volume":"111","author":"Grauwet","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1656","DOI":"10.1073\/pnas.0707883105","article-title":"Down-regulation of NKG2D and NKp80 ligands by Kaposi\u2019s sarcoma-associated herpesvirus K5 protects against NK cell cytotoxicity","volume":"105","author":"Thomas","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1016\/j.vetmic.2017.06.015","article-title":"Marek\u2019s disease virus type 1 encoded analog of miR-155 promotes proliferation of chicken embryo fibroblast and DF-1 cells by targeting hnRNPAB","volume":"207","author":"Dang","year":"2017","journal-title":"Vet. Microbiol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1016\/j.virol.2014.03.032","article-title":"Pseudorabies viral replication is inhibited by a novel target of miR-21","volume":"456\u2013457","author":"Huang","year":"2014","journal-title":"Virology"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1126\/science.1140956","article-title":"Host immune system gene targeting by a viral miRNA","volume":"317","author":"Elefant","year":"2007","journal-title":"Science"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1016\/j.chom.2009.03.003","article-title":"Diverse herpesvirus microRNAs target the stress-induced immune ligand MICB to escape recognition by natural killer cells","volume":"5","author":"Nachmani","year":"2009","journal-title":"Cell Host Microbe"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/j.vetmic.2010.02.017","article-title":"Herpesviruses and immunity: The art of evasion","volume":"143","author":"Griffin","year":"2010","journal-title":"Vet. Microbiol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/S0378-1135(96)01231-X","article-title":"Molecular virology of ruminant herpesviruses","volume":"53","author":"Schwyzer","year":"1996","journal-title":"Vet. Microbiol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/S0378-1135(96)01230-8","article-title":"Pathogenesis of ruminant herpesvirus infections","volume":"53","author":"Engels","year":"1996","journal-title":"Vet. Microbiol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"255","DOI":"10.3390\/v1020255","article-title":"Regulation of Innate Immune Responses by Bovine Herpesvirus 1 and Infected Cell Protein 0 (bICP0)","volume":"1","author":"Jones","year":"2009","journal-title":"Viruses"},{"key":"ref_67","doi-asserted-by":"crossref","unstructured":"Tesfaye Melkamsew, A., Sisay Tessema, T., and Paeshuyse, J. (2025). Host Immune Response to Bovine Viral Diarrhea Virus (BVDV): Insights and Strategies for Effective Vaccine Design. Vaccines, 13.","DOI":"10.20944\/preprints202501.0876.v1"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"564","DOI":"10.1016\/0264-410X(91)90243-Y","article-title":"Bovine herpesvirus-1 (infectious bovine rhinotracheitis virus)-based viral vector which expresses foot-and-mouth disease epitopes","volume":"9","author":"Kit","year":"1991","journal-title":"Vaccine"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"2839","DOI":"10.1099\/0022-1317-80-11-2839","article-title":"Expression of bovine viral diarrhoea virus glycoprotein E2 by bovine herpesvirus-1 from a synthetic ORF and incorporation of E2 into recombinant virions","volume":"80","author":"Schmitt","year":"1999","journal-title":"J. Gen. Virol."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"1159","DOI":"10.1007\/s10529-009-9988-2","article-title":"Construction of a recombinant BHV-1 expressing the VP1 gene of foot and mouth disease virus and its immunogenicity in a rabbit model","volume":"31","author":"Ren","year":"2009","journal-title":"Biotechnol. Lett."},{"key":"ref_71","doi-asserted-by":"crossref","unstructured":"Chowdhury, S.I., Pannhorst, K., Sangewar, N., Pavulraj, S., Wen, X., Stout, R.W., Mwangi, W., and Paulsen, D.B. (2021). BoHV-1-Vectored BVDV-2 Subunit Vaccine Induces BVDV Cross-Reactive Cellular Immune Responses and Protects against BVDV-2 Challenge. Vaccines, 9.","DOI":"10.3390\/vaccines9010046"},{"key":"ref_72","doi-asserted-by":"crossref","unstructured":"Zhao, C., Gao, J., Wang, Y., Ji, L., Qin, H., Hu, W., Wang, J., Fan, S., and Xiao, Y. (2022). A Novel Rabies Vaccine Based on a Recombinant Bovine Herpes Virus Type 1 Expressing Rabies Virus Glycoprotein. Front. Microbiol., 13.","DOI":"10.3389\/fmicb.2022.931043"},{"key":"ref_73","first-page":"309","article-title":"Role of gp63 and gIII of Aujeszky\u2019s disease virus in the invasion of the olfactory nervous pathway in neonatal pigs","volume":"42","author":"Kritas","year":"1994","journal-title":"Acta Vet. Hung."},{"key":"ref_74","first-page":"42","article-title":"Experiments to reduce the virulence of Aujeszky\u2019s virus","volume":"16","author":"Bartha","year":"1961","journal-title":"Magy. Allatorvosok Lapja"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"1.5.1","DOI":"10.1002\/0471142301.ns0105s68","article-title":"Transneuronal circuit analysis with pseudorabies viruses","volume":"68","author":"Card","year":"2014","journal-title":"Curr. Protoc. Neurosci."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1016\/j.vetimm.2005.03.008","article-title":"Protective immunity induced by a recombinant pseudorabies virus expressing the GP5 of porcine reproductive and respiratory syndrome virus in piglets","volume":"106","author":"Qiu","year":"2005","journal-title":"Vet. Immunol. Immunopathol."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/j.vetimm.2006.01.015","article-title":"A recombinant pseudorabies virus encoding the HA gene from H3N2 subtype swine influenza virus protects mice from virulent challenge","volume":"111","author":"Tian","year":"2006","journal-title":"Vet. Immunol. Immunopathol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"948","DOI":"10.1099\/vir.0.059253-0","article-title":"Immunization of pigs with an attenuated pseudorabies virus recombinant expressing the haemagglutinin of pandemic swine origin H1N1 influenza A virus","volume":"95","author":"Klingbeil","year":"2014","journal-title":"J. Gen. Virol."},{"key":"ref_79","doi-asserted-by":"crossref","unstructured":"Ren, J., Wang, H., Zhou, L., Ge, X., Guo, X., Han, J., Li, Y., Li, Y., Wang, Y., and An, T. (2020). Glycoproteins C and D of PRV Strain HB1201 Contribute Individually to the Escape From Bartha-K61 Vaccine-Induced Immunity. Front. Microbiol., 11.","DOI":"10.3389\/fmicb.2020.00323"},{"key":"ref_80","doi-asserted-by":"crossref","unstructured":"Zhang, C., Liu, Y., Chen, S., Qiao, Y., Guo, M., Zheng, Y., Xu, M., Wang, Z., Hou, J., and Wang, J. (2019). A gD&gC-substituted pseudorabies virus vaccine strain provides complete clinical protection and is helpful to prevent virus shedding against challenge by a Chinese pseudorabies variant. BMC Vet. Res., 15.","DOI":"10.1186\/s12917-018-1766-8"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/j.vetmic.2017.07.019","article-title":"Variations in glycoprotein B contribute to immunogenic difference between PRV variant JS-2012 and Bartha-K61","volume":"208","author":"Yu","year":"2017","journal-title":"Vet. Microbiol."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"101351","DOI":"10.1016\/j.lanmic.2026.101351","article-title":"Spillover of pseudorabies virus variants to humans: An urgent call for pseudorabies eradication in domestic pigs","volume":"7","author":"Wang","year":"2026","journal-title":"Lancet Microbe"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"001673","DOI":"10.1099\/jgv.0.001673","article-title":"ICTV Virus Taxonomy Profile: Herpesviridae 2021","volume":"102","author":"Gatherer","year":"2021","journal-title":"J. Gen. Virol."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1637\/11987-103018-Reg.1","article-title":"Study of Efficacy and Replication of Recombinant Vector Vaccines by Using Turkey Herpesvirus Combined with Other Marek\u2019s Disease Vaccines","volume":"63","author":"Gimeno","year":"2019","journal-title":"Avian Dis."},{"key":"ref_85","doi-asserted-by":"crossref","unstructured":"Wang, H., Tian, J., Zhao, J., Zhao, Y., Yang, H., and Zhang, G. (2024). Current Status of Poultry Recombinant Virus Vector Vaccine Development. Vaccines, 12.","DOI":"10.3390\/vaccines12060630"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/j.vetimm.2017.02.003","article-title":"Protective efficacy of a novel recombinant Marek\u2019s disease virus vector vaccine against infectious bursal disease in chickens with or without maternal antibodies","volume":"186","author":"Li","year":"2017","journal-title":"Vet. Immunol. Immunopathol."},{"key":"ref_87","doi-asserted-by":"crossref","unstructured":"Cui, H., Gao, H., Cui, X., Zhao, Y., Shi, X., Li, Q., Yan, S., Gao, Y., Wang, X., and Liu, C. (2013). Avirulent Marek\u2019s disease virus type 1 strain 814 vectored vaccine expressing avian influenza (AI) virus H5 haemagglutinin induced better protection than turkey herpesvirus vectored AI vaccine. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0053340"},{"key":"ref_88","doi-asserted-by":"crossref","unstructured":"Liu, Y., Li, K., Gao, Y., Gao, L., Zhong, L., Zhang, Y., Liu, C., Zhang, Y., and Wang, X. (2016). Recombinant Marek\u2019s Disease Virus as a Vector-Based Vaccine against Avian Leukosis Virus Subgroup J in Chicken. Viruses, 8.","DOI":"10.3390\/v8110301"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1637\/10966-103014-Reg","article-title":"Evaluation of the Protection Efficacy of a Serotype 1 Marek\u2019s Disease Virus-Vectored Bivalent Vaccine Against Infectious Laryngotracheitis and Marek\u2019s Disease","volume":"59","author":"Gimeno","year":"2015","journal-title":"Avian Dis."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1016\/j.tvjl.2004.04.018","article-title":"Equine herpesviruses 1 (EHV-1) and 4 (EHV-4)\u2014Epidemiology, disease and immunoprophylaxis: A brief review","volume":"170","author":"Patel","year":"2005","journal-title":"Vet. J."},{"key":"ref_91","first-page":"58","article-title":"Equine herpesvirus 1 and 4 infections: An update","volume":"24","year":"2002","journal-title":"Vet. Q."},{"key":"ref_92","first-page":"1","article-title":"Alterations in the equine herpesvirus type-1 (EHV-1) strain RacH during attenuation","volume":"43","author":"Birkenmaier","year":"1996","journal-title":"Zentralbl Vet. B"},{"key":"ref_93","first-page":"351","article-title":"Mutations in the US2 and glycoprotein B genes of the equine herpesvirus 1 vaccine strain RacH have no effects on its attenuation","volume":"112","author":"Neubauer","year":"1999","journal-title":"Berl. Munch. Tierarztl. Wochenschr."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1586\/14760584.5.1.119","article-title":"Equine herpesvirus type 1 modified live virus vaccines: Quo vaditis?","volume":"5","author":"Rosas","year":"2006","journal-title":"Expert Rev. Vaccines"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"748","DOI":"10.1099\/vir.0.82528-0","article-title":"Evaluation of the vaccine potential of an equine herpesvirus type 1 vector expressing bovine viral diarrhea virus structural proteins","volume":"88","author":"Rosas","year":"2007","journal-title":"J. Gen. Virol."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/j.virusres.2006.12.009","article-title":"Live-attenuated recombinant equine herpesvirus type 1 (EHV-1) induces a neutralizing antibody response against West Nile virus (WNV)","volume":"125","author":"Rosas","year":"2007","journal-title":"Virus Res."},{"key":"ref_97","doi-asserted-by":"crossref","unstructured":"Ma, G., Eschbaumer, M., Said, A., Hoffmann, B., Beer, M., and Osterrieder, N. (2012). An equine herpesvirus type 1 (EHV-1) expressing VP2 and VP5 of serotype 8 bluetongue virus (BTV-8) induces protection in a murine infection model. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0034425"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"2335","DOI":"10.1016\/j.vaccine.2008.02.064","article-title":"Evaluation of a vectored equine herpesvirus type 1 (EHV-1) vaccine expressing H3 haemagglutinin in the protection of dogs against canine influenza","volume":"26","author":"Rosas","year":"2008","journal-title":"Vaccine"},{"key":"ref_99","doi-asserted-by":"crossref","unstructured":"Pradhan, S.S., Balena, V., Bera, B.C., Anand, T., Khetmalis, R., Madhwal, A., Kandasamy, S., Pavulraj, S., Bernela, M., and Mor, P. (2025). Multiple Gene Deletion Mutants of Equine Herpesvirus 1 Exhibit Strong Protective Efficacy Against Wild Virus Challenge in a Murine Model. Vaccines, 13.","DOI":"10.3390\/vaccines13010045"},{"key":"ref_100","first-page":"384","article-title":"Duck virus enterities","volume":"12","author":"Fadly","year":"2008","journal-title":"Dis. Poult."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"461","DOI":"10.2307\/1592206","article-title":"Inactivated vaccine for protection against duck virus enteritis","volume":"41","author":"Shawky","year":"1997","journal-title":"Avian Dis."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1007\/s00705-014-2275-0","article-title":"Biological properties of a duck enteritis virus attenuated via serial passaging in chick embryo fibroblasts","volume":"160","author":"Yang","year":"2015","journal-title":"Arch. Virol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1080\/01652176.2017.1298885","article-title":"Duck virus enteritis (duck plague)\u2014A comprehensive update","volume":"37","author":"Dhama","year":"2017","journal-title":"Vet. Q."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1186\/1743-422X-8-200","article-title":"Different linkages in the long and short regions of the genomes of duck enteritis virus Clone-03 and VAC strains","volume":"8","author":"Liu","year":"2011","journal-title":"Virol. J."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/j.antiviral.2012.12.015","article-title":"Recombinant duck enteritis virus works as a single-dose vaccine in broilers providing rapid protection against H5N1 influenza infection","volume":"97","author":"Liu","year":"2013","journal-title":"Antivir. Res."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1186\/s13567-015-0174-3","article-title":"Efficient strategy for constructing duck enteritis virus-based live attenuated vaccine against homologous and heterologous H5N1 avian influenza virus and duck enteritis virus infection","volume":"46","author":"Zou","year":"2015","journal-title":"Vet. Res."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1186\/s12985-015-0354-9","article-title":"Construction of a recombinant duck enteritis virus (DEV) expressing hemagglutinin of H5N1 avian influenza virus based on an infectious clone of DEV vaccine strain and evaluation of its efficacy in ducks and chickens","volume":"12","author":"Wang","year":"2015","journal-title":"Virol. J."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"5271","DOI":"10.1016\/j.vaccine.2014.07.082","article-title":"The vaccine efficacy of recombinant duck enteritis virus expressing secreted E with or without PrM proteins of duck tembusu virus","volume":"32","author":"Chen","year":"2014","journal-title":"Vaccine"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"2428","DOI":"10.3390\/v6062428","article-title":"Efficient strategy to generate a vectored duck enteritis virus delivering envelope of duck Tembusu virus","volume":"6","author":"Zou","year":"2014","journal-title":"Viruses"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.antiviral.2016.03.003","article-title":"Recombinant duck enteritis viruses expressing major structural proteins of the infectious bronchitis virus provide protection against infectious bronchitis in chickens","volume":"130","author":"Li","year":"2016","journal-title":"Antivir. Res."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1007\/s00705-016-3077-3","article-title":"Construction of a recombinant duck enteritis virus vaccine expressing hemagglutinin of H9N2 avian influenza virus and evaluation of its efficacy in ducks","volume":"162","author":"Sun","year":"2017","journal-title":"Arch. Virol."},{"key":"ref_112","doi-asserted-by":"crossref","unstructured":"Bo, Z., and Li, X. (2022). A Review of Pseudorabies Virus Variants: Genomics, Vaccination, Transmission, and Zoonotic Potential. Viruses, 14.","DOI":"10.3390\/v14051003"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/j.neuropharm.2016.02.013","article-title":"Viral vectors for therapy of neurologic diseases","volume":"120","author":"Choudhury","year":"2017","journal-title":"Neuropharmacology"},{"key":"ref_114","unstructured":"University of Alabama at Birmingham (2025). Clinical Trial Genetically Engineered HSV-1 Phase 1 Study for the Treatment of Recurrent Malignant Glioma (M032-HSV-1), University of Alabama at Birmingham."},{"key":"ref_115","doi-asserted-by":"crossref","unstructured":"Yudaeva, A., Kostyusheva, A., Kachanov, A., Brezgin, S., Ponomareva, N., Parodi, A., Pokrovsky, V.S., Lukashev, A., Chulanov, V., and Kostyushev, D. (2024). Clinical and Translational Landscape of Viral Gene Therapies. Cells, 13.","DOI":"10.3390\/cells13221916"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"201100","DOI":"10.1016\/j.omton.2025.201100","article-title":"Viral warriors: Unlocking the immune system\u2019s potential with oncolytic viruses in cancer immunotherapy","volume":"33","author":"Ghavimi","year":"2025","journal-title":"Mol. Ther. Oncol."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s40257-016-0238-9","article-title":"Talimogene Laherparepvec (T-VEC) and Other Oncolytic Viruses for the Treatment of Melanoma","volume":"18","author":"Bommareddy","year":"2017","journal-title":"Am. J. Clin. Dermatol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1016\/j.conb.2009.03.007","article-title":"Transneuronal circuit tracing with neurotropic viruses","volume":"18","author":"Callaway","year":"2008","journal-title":"Curr. Opin. Neurobiol."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/j.molmed.2007.12.008","article-title":"The alpha-herpesviruses: Molecular pathfinders in nervous system circuits","volume":"14","author":"Ekstrand","year":"2008","journal-title":"Trends Mol. Med."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"S209","DOI":"10.1086\/344278","article-title":"Exploiting Circuit-Specific Spread of Pseudorabies Virus in the Central Nervous System: Insights to Pathogenesis and Circuit Tracers","volume":"186","author":"Enquist","year":"2002","journal-title":"J. Infect. Dis."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.virusres.2017.01.011","article-title":"Bovine herpesvirus 1 can efficiently infect the human (SH-SY5Y) but not the mouse neuroblastoma cell line (Neuro-2A)","volume":"232","author":"Thunuguntla","year":"2017","journal-title":"Virus Res."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"5445","DOI":"10.1128\/JVI.79.9.5445-5454.2005","article-title":"Potential of equine herpesvirus 1 as a vector for immunization","volume":"79","author":"Trapp","year":"2005","journal-title":"J. Virol."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/27\/13\/5686\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,6,27]],"date-time":"2026-06-27T04:47:48Z","timestamp":1782535668000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/27\/13\/5686"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,6,24]]},"references-count":122,"journal-issue":{"issue":"13","published-online":{"date-parts":[[2026,7]]}},"alternative-id":["ijms27135686"],"URL":"https:\/\/doi.org\/10.3390\/ijms27135686","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,6,24]]}}}