{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,25]],"date-time":"2026-04-25T03:20:16Z","timestamp":1777087216986,"version":"3.51.4"},"reference-count":89,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2020,3,24]],"date-time":"2020-03-24T00:00:00Z","timestamp":1585008000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Microorganisms"],"abstract":"<jats:p>Vast evolutionary distances separate the known herpesviruses, adapted to colonise specialised cells in predominantly vertebrate hosts. Nevertheless, the distinct herpesvirus families share recognisably related genomic attributes. The taxonomic Family Herpesviridae includes many important human and animal pathogens. Successful antiviral drugs targeting Herpesviridae are available, but the need for reduced toxicity and improved efficacy in critical healthcare interventions invites novel solutions: immunocompromised patients presenting particular challenges. A conserved enzyme required for viral fitness is Ung, a uracil-DNA glycosylase, which is encoded ubiquitously in Herpesviridae genomes and also host cells. Research investigating Ung in Herpesviridae dynamics has uncovered an unexpected combination of viral co-option of host Ung, along with remarkable Subfamily-specific exaptation of the virus-encoded Ung. These enzymes apparently play essential roles, both in the maintenance of viral latency and during initiation of lytic replication. The ubiquitously conserved Ung active site has previously been explored as a therapeutic target. However, exquisite selectivity and better drug-like characteristics might instead be obtained via targeting structural variations within another motif of catalytic importance in Ung. The motif structure is unique within each Subfamily and essential for viral survival. This unique signature in highly conserved Ung constitutes an attractive exploratory target for the development of novel beneficial therapeutics.<\/jats:p>","DOI":"10.3390\/microorganisms8030461","type":"journal-article","created":{"date-parts":[[2020,3,24]],"date-time":"2020-03-24T13:04:04Z","timestamp":1585055044000},"page":"461","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["The Essential Co-Option of Uracil-DNA Glycosylases by Herpesviruses Invites Novel Antiviral Design"],"prefix":"10.3390","volume":"8","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7375-2340","authenticated-orcid":false,"given":"Renos","family":"Savva","sequence":"first","affiliation":[{"name":"Institute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck, University of London, Malet Street, London WC1E 7HX, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2020,3,24]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Arvin, A., Campadelli-Fiume, G., Mocarski, E., Moore, P.S., Roizman, B., Whitley, R., and Yamanishi, K. (2007). Human Herpesviruses\u2014Biology, Therapy, and Immunoprophylaxis, Cambridge University Press. ISBN-13: 978-0-521-82714-0.","DOI":"10.1017\/CBO9780511545313"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1093\/bmb\/ldt011","article-title":"Recent developments in anti-herpesvirus drugs","volume":"106","author":"Field","year":"2013","journal-title":"Br. Med. Bull."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1017\/S002572730002737X","article-title":"The Origin and the Use of the Word Herpes","volume":"6","author":"Beswick","year":"1962","journal-title":"Med. Hist."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/j.coviro.2014.09.010","article-title":"Chromosomally integrated HHV-6: Impact on virus, cell and organismal biology","volume":"9","author":"Kaufer","year":"2014","journal-title":"Curr. Opin. Virol."},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Agut, H., Bonnafous, P., and Gautheret-Dejean, A. (2016). Human herpesviruses 6A, 6B, and 7. Microbiol. Spectrum., 4.","DOI":"10.1128\/microbiolspec.DMIH2-0007-2015"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"596","DOI":"10.1001\/archneur.65.5.596","article-title":"Neurological Complications of Herpes Simplex Virus Type 2 Infection","volume":"65","author":"Berger","year":"2008","journal-title":"Arch. Neurol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"177","DOI":"10.3389\/fcimb.2018.00177","article-title":"Herpesviruses: Harmonious Pathogens but Relevant Cofactors in Other Diseases?","volume":"25","author":"Sehrawat","year":"2018","journal-title":"Front. Cell Infect. Microbiol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1016\/S1473-3099(11)70024-X","article-title":"Maribavir prophylaxis for prevention of cytomegalovirus disease in recipients of allogeneic stem-cell transplants: A phase 3, double-blind, placebo-controlled, randomised trial","volume":"11","author":"Marty","year":"2011","journal-title":"Lancet Infect. Dis."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1038\/362709a0","article-title":"Instability and decay of the primary structure of DNA","volume":"362","author":"Lindahl","year":"1993","journal-title":"Nature"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"2358","DOI":"10.1021\/bi00871a026","article-title":"The deamination of cytidine and cytosine by acidic buffer solutions. Mutagenic implications","volume":"5","author":"Shapiro","year":"1966","journal-title":"Biochemistry"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"3405","DOI":"10.1021\/bi00713a035","article-title":"Heat-induced deamination of cytosine residues in deoxyribonucleic acid","volume":"13","author":"Lindahl","year":"1974","journal-title":"Biochemistry"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"3535","DOI":"10.1021\/bi00065a003","article-title":"Kinetics of bisulfite-induced cytosine deamination in single-stranded DNA","volume":"32","author":"Chen","year":"1993","journal-title":"Biochemistry"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1016\/0165-1110(90)90019-8","article-title":"Spontaneous deamination of cytosine and 5-methylcytosine residues in DNA and replacement of 5-methylcytosine residues with cytosine residues","volume":"238","author":"Ehrlich","year":"1990","journal-title":"Mutat. Res."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"972","DOI":"10.1093\/nar\/22.6.972","article-title":"The rate of hydrolytic deamination of 5-methylcytosine in double-stranded DNA","volume":"22","author":"Shen","year":"1994","journal-title":"Nucleic Acids Res."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"9733","DOI":"10.1128\/JVI.00694-10","article-title":"Viral Mutation Rates","volume":"84","author":"Nebot","year":"2010","journal-title":"J. Virol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"e01031-e17","DOI":"10.1128\/JVI.01031-17","article-title":"Complexities of Viral Mutation Rates","volume":"92","author":"Peck","year":"2018","journal-title":"J. Virol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.dnarep.2019.02.014","article-title":"Deoxyuracil in DNA and disease: Genomic signal or managed situation?","volume":"77","author":"Chon","year":"2019","journal-title":"DNA Repair (Amst.)"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1021\/ar800114w","article-title":"Keeping Uracil Out of DNA: Physiological Role, Structure and Catalytic Mechanism of dUTPases","volume":"42","year":"2009","journal-title":"Acc. Chem. Res."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"e349","DOI":"10.1038\/oncsis.2017.46","article-title":"Limited nucleotide pools restrict Epstein\u2013Barr virus-mediated B-cell immortalization","volume":"6","author":"Hafez","year":"2017","journal-title":"Oncogenesis"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"7941","DOI":"10.1128\/JVI.72.10.7941-7949.1998","article-title":"Deoxyribonucleoside triphosphate pool imbalances in vivo are associated with an increased retroviral mutation rate","volume":"72","author":"Julias","year":"1998","journal-title":"J. Virol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1016\/j.virol.2004.05.010","article-title":"Evidence that the human cytomegalovirus 46-kDa UL72 protein is not an active dUTPase but a late protein dispensable for replication in fibroblasts","volume":"325","author":"Caposio","year":"2004","journal-title":"Virology"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"9975","DOI":"10.1093\/nar\/15.23.9975","article-title":"Thymine methyls and DNA-protein interactions","volume":"15","author":"Ivarie","year":"1987","journal-title":"Nucleic Acids Res."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"5775","DOI":"10.1093\/nar\/18.19.5775","article-title":"The specific binding of nuclear protein(s) to the cAMP responsive element (CRE) sequence (TGACGTCA) is reduced by the misincorporation of U and increased by the deamination of C","volume":"18","author":"Verri","year":"1990","journal-title":"Nucleic Acids Res."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"S67","DOI":"10.1007\/BF02451788","article-title":"Uracil in OriS of herpes simplex 1 alters its specific recognition by origin binding protein (OBP): Does virus induced uracil-DNA glycosylase play a key role in viral reactivation and replication?","volume":"102","author":"Focher","year":"1992","journal-title":"Chromosoma"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1667","DOI":"10.1002\/pro.2554","article-title":"Uracil-DNA glycosylases \u2014 Structural and functional perspectives on an essential family of DNA repair enzymes","volume":"23","author":"Schormann","year":"2014","journal-title":"Protein Sci."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1073\/pnas.74.1.154","article-title":"Transient accumulation of Okazaki fragments as a result of uracil incorporation into nascent DNA","volume":"74","author":"Tye","year":"1977","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"250","DOI":"10.3389\/fmicb.2012.00250","article-title":"Antiviral mechanism and biochemical basis of the human APOBEC3 family","volume":"3","author":"Imahashi","year":"2012","journal-title":"Front. Microbiol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"11667","DOI":"10.1074\/jbc.M606864200","article-title":"Virion-associated Uracil DNA Glycosylase-2 and Apurinic\/ Apyrimidinic Endonuclease Are Involved in the Degradation of APOBEC3G-edited Nascent HIV-1 DNA","volume":"282","author":"Yang","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/j.coi.2006.03.007","article-title":"Somatic hypermutation: Subverted DNA repair","volume":"18","author":"Martomo","year":"2006","journal-title":"Curr. Opin. Immunol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"E1016","DOI":"10.1073\/pnas.1402391111","article-title":"Differential regulation of S-region hypermutation and class-switch recombination by noncanonical functions of uracil DNA glycosylase","volume":"111","author":"Yousif","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"9244","DOI":"10.1073\/pnas.1102943108","article-title":"HIV DNA is heavily uracilated, which protects it from autointegration","volume":"108","author":"Yan","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"E448","DOI":"10.1073\/pnas.1219702110","article-title":"Uracil DNA glycosylase initiates degradation of HIV-1 cDNA containing misincorporated dUTP and prevents viral integration","volume":"110","author":"Weil","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"e18447","DOI":"10.7554\/eLife.18447","article-title":"Diverse fates of uracilated HIV-1 DNA during infection of myeloid lineage cells","volume":"5","author":"Hansen","year":"2016","journal-title":"Elife"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"794","DOI":"10.1038\/197794a0","article-title":"Replacement of Thymidylic Acid by Deoxyuridylic Acid in the Deoxyribonucleic Acid of a Transducing Phage for Bacillus subtilis","volume":"197","author":"Takahashi","year":"1963","journal-title":"Nature"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"4093","DOI":"10.1099\/mic.0.28265-0","article-title":"Yersiniophage \u03d5R1-37 is a tailed bacteriophage having a 270 kb DNA genome with thymidine replaced by deoxyuridine","volume":"151","author":"Kiljunen","year":"2005","journal-title":"Microbiology"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1949","DOI":"10.1038\/ismej.2014.29","article-title":"Intragenus generalized transduction in Staphylococcus spp. by a novel giant phage","volume":"8","author":"Uchiyama","year":"2014","journal-title":"ISME J."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/j.virol.2016.04.030","article-title":"The genome of AR9, a giant transducing Bacillus phage encoding two multisubunit RNA polymerases","volume":"495","author":"Lavysh","year":"2016","journal-title":"Virology"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"835","DOI":"10.1128\/jvi.22.3.835-838.1977","article-title":"Metabolism of uracil-containing DNA: Degradation of bacteriophage PBS2 DNA in Bacillus subtilis","volume":"22","author":"Duncan","year":"1977","journal-title":"J. Virol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"3649","DOI":"10.1073\/pnas.71.9.3649","article-title":"An N-glycosidase from Escherichia coli that releases free uracil from DNA containing deaminated cytosine residues","volume":"71","author":"Lindahl","year":"1974","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"2113","DOI":"10.1002\/pro.3058","article-title":"Poxvirus uracil-DNA glycosylase-An unusual member of the family I uracil-DNA glycosylases","volume":"25","author":"Schormann","year":"2016","journal-title":"Protein Sci."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1323","DOI":"10.4155\/fmc-2018-0319","article-title":"Targeting uracil-DNA glycosylases for therapeutic outcomes using insights from virus evolution","volume":"11","author":"Savva","year":"2019","journal-title":"Future Med. Chem."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"4963","DOI":"10.1128\/jvi.68.8.4963-4972.1994","article-title":"Evidence that the herpes simplex virus type 1 uracil DNA glycosylase is required for efficient viral replication and latency in the murine nervous system","volume":"68","author":"Pyles","year":"1994","journal-title":"J. Virol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1038\/373487a0","article-title":"The structural basis of specific base-excision repair by uracil-DNA glycosylase","volume":"373","author":"Savva","year":"1995","journal-title":"Nature"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"3018","DOI":"10.1128\/jvi.70.5.3018-3025.1996","article-title":"Human cytomegalovirus uracil DNA glycosylase is required for the normal temporal regulation of both DNA synthesis and viral replication","volume":"70","author":"Prichard","year":"1996","journal-title":"J. Virol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"7592","DOI":"10.1128\/JVI.75.16.7592-7601.2001","article-title":"Requirement for Uracil-DNA Glycosylase during the Transition to Late-Phase Cytomegalovirus DNA Replication","volume":"75","author":"Courcelle","year":"2001","journal-title":"J. Virol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1186\/1743-422X-2-55","article-title":"Human cytomegalovirus uracil DNA glycosylase associates with ppUL44 and accelerates the accumulation of viral DNA","volume":"2","author":"Prichard","year":"2005","journal-title":"Virol. J."},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Ranneberg-Nilsen, T., Rollag, H., Slettebakk, R., Backe, P.H., Olsen, \u00d8., Luna, L., and Bj\u00f8r\u00e5s, M. (2012). The chromatin remodeling factor smarcb1 forms a complex with human cytomegalovirus proteins UL114 and UL44. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0034119"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"2029","DOI":"10.1099\/vir.0.022160-0","article-title":"Interaction of the human cytomegalovirus uracil DNA glycosylase UL114 with the viral DNA polymerase catalytic subunit UL54","volume":"91","author":"Strang","year":"2010","journal-title":"J. Gen. Virol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1195","DOI":"10.1128\/JVI.01518-06","article-title":"Characterization of the uracil-DNA glycosylase activity of Epstein-Barr virus BKRF3 and its role in lytic viral DNA replication","volume":"81","author":"Lu","year":"2007","journal-title":"J. Virol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"8883","DOI":"10.1128\/JVI.00950-14","article-title":"Uracil DNA glycosylase BKRF3 contributes to Epstein-Barr virus DNA replication through physical interactions with proteins in viral DNA replication complex","volume":"88","author":"Su","year":"2014","journal-title":"J. Virol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/j.jmb.2006.11.007","article-title":"New insights on the role of the gamma-herpesvirus uracil-DNA glycosylase leucine loop revealed by the structure of the Epstein-Barr virus enzyme in complex with an inhibitor protein","volume":"366","author":"Buisson","year":"2007","journal-title":"J. Mol. Biol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"4286","DOI":"10.1093\/nar\/gky217","article-title":"A structurally conserved motif in \u03b3-herpesvirus uracil-DNA glycosylases elicits duplex nucleotide-flipping","volume":"46","author":"Earl","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"10256","DOI":"10.1128\/JVI.02654-08","article-title":"Human immunodeficiency virus type 1 Vpr modulates cellular expression of UNG2 via a negative transcriptional effect","volume":"83","author":"Langevin","year":"2009","journal-title":"J. Virol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1128\/jvi.70.2.697-704.1996","article-title":"Human immunodeficiency virus type 1 Vpr protein binds to the uracil DNA glycosylase DNA repair enzyme","volume":"70","author":"Bouhamdan","year":"1996","journal-title":"J. Virol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1698","DOI":"10.1093\/nar\/gkt974","article-title":"Vpr expression abolishes the capacity of HIV-1 infected cells to repair uracilated DNA","volume":"42","author":"Eldin","year":"2013","journal-title":"Nucleic Acids Res."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"10978","DOI":"10.1128\/JVI.79.17.10978-10987.2005","article-title":"Human immunodeficiency virus type 1 Vpr induces the degradation of the UNG and SMUG uracil-DNA glycosylases","volume":"79","author":"Yu","year":"2005","journal-title":"J. Virol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1128\/jvi.20.2.535-538.1976","article-title":"Bacteriophage PBS2-induced inhibition of uracil-containing DNA degradation","volume":"20","author":"Katz","year":"1976","journal-title":"J. Virol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1163","DOI":"10.1016\/S0021-9258(19)85067-6","article-title":"UraciI-DNA glycosylase inhibitor gene of bacteriophage PBS2 encodes a binding protein specific for uraciI-DNA glycosylase","volume":"264","author":"Wang","year":"1989","journal-title":"J. Biol. Chem."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1128\/jvi.33.1.535-538.1980","article-title":"Early Events After Infection of Escherichia coli by Bacteriophage T5. III. Inhibition of Uracil-DNA Glycosylase Activity","volume":"33","author":"Warner","year":"1980","journal-title":"J. Virol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"19044","DOI":"10.1073\/pnas.0808797105","article-title":"Phage \u03c629 protein p56 prevents viral DNA replication impairment caused by uracil excision activity of uracil-DNA glycosylase","volume":"105","author":"Bravo","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1016\/S0022-2836(68)80018-X","article-title":"Single Strand Interruptions in PBS 1 Bacteriophage DNA Molecule","volume":"35","author":"Yamagishi","year":"1968","journal-title":"J. Mol. Biol."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1128\/jvi.23.3.737-750.1977","article-title":"Localization of single-chain interruptions in bacteriophage T5 DNA. II. Electrophoretic studies","volume":"23","author":"Rhoades","year":"1977","journal-title":"J. Virol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"e51163","DOI":"10.1371\/journal.pone.0051163","article-title":"Genomic Analysis of Pseudomonas putida Phage tf with Localized Single-Strand DNA Interruptions","volume":"7","author":"Glukhov","year":"2012","journal-title":"PLoS ONE"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/S0027-5107(01)00149-X","article-title":"Bisulfite-induced cytosine deamination rates in E. coli SSB:DNA complexes","volume":"478","author":"Lough","year":"2001","journal-title":"Mutat. Res."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/S0065-2776(06)94002-4","article-title":"DNA deamination in immunity: AID in the context of its APOBEC relatives","volume":"94","author":"Conticello","year":"2007","journal-title":"Adv. Immunol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1552","DOI":"10.1002\/pro.3670","article-title":"APOBEC3s: DNA-editing human cytidine deaminases","volume":"28","author":"Silvas","year":"2019","journal-title":"Protein Sci."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"e01224-18","DOI":"10.1128\/JVI.01224-18","article-title":"Strategy of Human Cytomegalovirus To Escape Interferon Beta-Induced APOBEC3G Editing Activity","volume":"92","author":"Pautasso","year":"2018","journal-title":"J. Virol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1038\/s41564-018-0284-6","article-title":"Epstein\u2013Barr virus BORF2 inhibits cellular APOBEC3B to preserve viral genome integrity","volume":"4","author":"Cheng","year":"2019","journal-title":"Nat. Microbiol"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"11178","DOI":"10.1128\/JVI.01334-06","article-title":"Latency-associated nuclear antigen of Kaposi\u2019s sarcoma-associated herpesvirus recruits uracil DNA glycosylase 2 at the terminal repeats and is important for latent persistence of the virus","volume":"80","author":"Verma","year":"2006","journal-title":"J. Virol."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"8760","DOI":"10.1093\/nar\/gkt633","article-title":"Architecturally diverse proteins converge on an analogous mechanism to inactivate Uracil-DNA glycosylase","volume":"41","author":"Cole","year":"2013","journal-title":"Nucleic Acids Res."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"1354","DOI":"10.1093\/nar\/gkt964","article-title":"Staphylococcus aureus protein SAUGI acts as a uracil-DNA glycosylase inhibitor","volume":"42","author":"Wang","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"933","DOI":"10.1038\/nsmb.3284","article-title":"The DDB1\u2013DCAF1\u2013Vpr\u2013UNG2 crystal structure reveals how HIV-1 Vpr steers human UNG2 toward destruction","volume":"23","author":"Wu","year":"2016","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"923","DOI":"10.1002\/bip.22347","article-title":"Fifty years of DNA \u201cBreathing\u201d: Reflections on old and new approaches","volume":"99","author":"Johnson","year":"2013","journal-title":"Biopolymers"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"5214","DOI":"10.1093\/emboj\/17.17.5214","article-title":"Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA","volume":"17","author":"Parikh","year":"1998","journal-title":"EMBO J."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1038\/nature06131","article-title":"Enzymatic capture of an extrahelical thymine in the search for uracil in DNA","volume":"449","author":"Parker","year":"2007","journal-title":"Nature"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"4440","DOI":"10.1093\/nar\/gkw185","article-title":"Using structural-based protein engineering to modulate the differential inhibition effects of SAUGI on human and HSV uracil DNA glycosylase","volume":"44","author":"Wang","year":"2016","journal-title":"Nucleic Acids Res."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"3366","DOI":"10.1128\/JVI.03111-14","article-title":"Absence of the uracil DNA glycosylase of murine gammaherpesvirus 68 impairs replication and delays the establishment of latency in vivo","volume":"89","author":"Minkah","year":"2015","journal-title":"J. Virol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1099\/0022-1317-70-2-449","article-title":"Gene UL2 of herpes simplex virus type 1 encodes a uracil-DNA glycosylase","volume":"70","author":"Mullaney","year":"1989","journal-title":"J. Gen. Virol."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"27664","DOI":"10.1074\/jbc.M110.131235","article-title":"Association between the Herpes Simplex Virus-1 DNA Polymerase and Uracil DNA Glycosylase","volume":"285","author":"Bogani","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"e00295-19","DOI":"10.1128\/mSystems.00295-19","article-title":"Conserved Central Intraviral Protein Interactome of the Herpesviridae Family","volume":"4","author":"Topf","year":"2019","journal-title":"mSystems"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"806","DOI":"10.1038\/s41467-020-14586-5","article-title":"Temporal dynamics of protein complex formation and dissociation during human cytomegalovirus infection","volume":"11","author":"Hashimoto","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1006\/viro.1995.1406","article-title":"Herpes simplex virus type 1 (HSV-1) uracil-DNA glycosylase: Functional expression in Escherichia coli, biochemical characterization, and selective inhibition by 6-(p-n-octylanilino)uracil","volume":"211","author":"Argnani","year":"1995","journal-title":"Virology"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"2344","DOI":"10.1021\/jm980718d","article-title":"Molecular Modeling and Synthesis of Inhibitors of Herpes Simplex Virus Type 1 Uracil-DNA Glycosylase","volume":"42","author":"Sun","year":"1999","journal-title":"J. Med. Chem."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"36506","DOI":"10.1074\/jbc.C000585200","article-title":"Selective inhibition of herpes simplex virus type-1 uracil-DNA glycosylase by designed substrate analogs","volume":"275","author":"Sekino","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"17412","DOI":"10.1021\/ja055846n","article-title":"Uracil-directed ligand tethering: An efficient strategy for uracil DNA glycosylase (UNG) inhibitor development","volume":"127","author":"Jiang","year":"2005","journal-title":"J. Am. Chem. Soc."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"3362","DOI":"10.1021\/ci500375a","article-title":"Computational Rationale for the Selective Inhibition of the Herpes Simplex Virus Type 1 Uracil-DNA Glycosylase Enzyme","volume":"54","author":"Hendricks","year":"2014","journal-title":"J. Chem. Inf. Model."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"e01831-18","DOI":"10.1128\/mBio.01831-18","article-title":"Combinatorial Loss of the Enzymatic Activities of Viral Uracil-DNA Glycosylase and Viral dUTPase Impairs Murine Gammaherpesvirus Pathogenesis and Leads to Increased Recombination-Based Deletion in the Viral Genome","volume":"9","author":"Dong","year":"2018","journal-title":"mBio"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"5872","DOI":"10.1093\/nar\/gkl747","article-title":"Mimicking damaged DNA with a small molecule inhibitor of human UNG2","volume":"34","author":"Krosky","year":"2006","journal-title":"Nucleic Acids Res."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"5666","DOI":"10.1016\/j.bmc.2006.04.022","article-title":"Synthesis and high-throughput evaluation of triskelion uracil libraries for inhibition of human dUTPase and UNG2","volume":"14","author":"Jiang","year":"2006","journal-title":"Bioorg. Med. Chem."}],"container-title":["Microorganisms"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-2607\/8\/3\/461\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T09:11:14Z","timestamp":1760173874000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-2607\/8\/3\/461"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,3,24]]},"references-count":89,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2020,3]]}},"alternative-id":["microorganisms8030461"],"URL":"https:\/\/doi.org\/10.3390\/microorganisms8030461","relation":{},"ISSN":["2076-2607"],"issn-type":[{"value":"2076-2607","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,3,24]]}}}