{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,30]],"date-time":"2026-07-30T12:29:07Z","timestamp":1785414547394,"version":"3.56.0"},"reference-count":160,"publisher":"MDPI AG","issue":"7","license":[{"start":{"date-parts":[[2026,7,7]],"date-time":"2026-07-07T00:00:00Z","timestamp":1783382400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Deakin University Postdoctoral Research Fellowship 2025"},{"id":[{"id":"https:\/\/ror.org\/02czsnj07","id-type":"ROR","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Pathogens"],"abstract":"<jats:p>Ubiquitination is a post-translational modification that governs various facets of eukaryotic biology, including protein stability, signaling, and immune regulation. The modification process is mediated by a coordinated enzymatic cascade, in which E3 ubiquitin ligases confer substrate specificity and determine the functional outcome of ubiquitin attachment. In the case of a virus infection, host cellular signaling networks undergo major ubiquitin-dependent changes to protect the host cell, including remodeling of cellular organelles, coordination of innate immunity, and reprogramming of metabolic pathways to prevent virus replication. African swine fever virus (ASFV) has evolved numerous strategies to counteract or evade these responses, thereby manipulating host defenses and promoting its replication. By modulating ubiquitination-dependent host cellular functions, the virus can regulate key immune signaling factors, suppress interferon production, and interfere with inflammatory pathways. These actions not only antagonize antiviral defenses but also remodel cellular homeostasis to favor infection. The important interplay between host defense and viral manipulation underscores the versatility of the ubiquitin system as a battleground in ASFV infection. In this review, we discussed mechanistic insights into how ASFV subverts ubiquitin pathways during host\u2013virus interactions. This comprehensive knowledge might be beneficial for pharmaceutical exploration of host E3 ligase-dependent anti-ASFV treatment.<\/jats:p>","DOI":"10.3390\/pathogens15070716","type":"journal-article","created":{"date-parts":[[2026,7,7]],"date-time":"2026-07-07T13:19:31Z","timestamp":1783430371000},"page":"716","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Exploiting Ubiquitination: African Swine Fever Virus-Mediated Recruitment of Host E3 Ligases During Viral Infection and Immune Regulation"],"prefix":"10.3390","volume":"15","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0279-2895","authenticated-orcid":false,"given":"Kiramage","family":"Chathuranga","sequence":"first","affiliation":[{"name":"School of Medicine, Deakin University, Geelong 3216, Australia"},{"name":"Institute for Mental and Physical Health and Clinical Translation (IMPACT), Deakin University, Geelong 3216, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8348-727X","authenticated-orcid":false,"given":"W. A. Gayan","family":"Chathuranga","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, College of Medicine, University of Illinois, Chicago, IL 60612, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5810-8063","authenticated-orcid":false,"given":"Tania F.","family":"de Koning-Ward","sequence":"additional","affiliation":[{"name":"School of Medicine, Deakin University, Geelong 3216, Australia"},{"name":"Institute for Mental and Physical Health and Clinical Translation (IMPACT), Deakin University, Geelong 3216, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5119-0711","authenticated-orcid":false,"given":"Jong-Soo","family":"Lee","sequence":"additional","affiliation":[{"name":"College of Veterinary Medicine, Chungnam National University, Daejeon 34134, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,7,7]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Njau, E.P., Machuka, E.M., Cleaveland, S., Shirima, G.M., Kusiluka, L.J., Okoth, E.A., and Pelle, R. (2021). African Swine Fever Virus (ASFV): Biology, Genomics and Genotypes Circulating in Sub-Saharan Africa. Viruses, 13.","DOI":"10.3390\/v13112285"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"2457949","DOI":"10.1080\/21505594.2025.2457949","article-title":"Insights and progress on epidemic characteristics, pathogenesis, and preventive measures of African swine fever virus: A review","volume":"16","author":"Li","year":"2025","journal-title":"Virulence"},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Chathuranga, K., and Lee, J.S. (2023). African Swine Fever Virus (ASFV): Immunity and Vaccine Development. Vaccines, 11.","DOI":"10.3390\/vaccines11020199"},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"Wang, G., Xie, M., Wu, W., and Chen, Z. (2021). Structures and Functional Diversities of ASFV Proteins. Viruses, 13.","DOI":"10.3390\/v13112124"},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Ambagala, A., Goonewardene, K., Kanoa, I.E., Than, T.T., Nguyen, V.T., Lai, T.N.H., Nguyen, T.L., Erdelyan, C.N.G., Robert, E., and Tailor, N. (2024). Characterization of an African Swine Fever Virus Field Isolate from Vietnam with Deletions in the Left Variable Multigene Family Region. Viruses, 16.","DOI":"10.3390\/v16040571"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1038\/s41541-023-00669-z","article-title":"Assessment of African swine fever vaccine candidate ASFV-G-\u2206MGF in a reversion to virulence study","volume":"8","author":"Deutschmann","year":"2023","journal-title":"npj Vaccines"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"14919","DOI":"10.1038\/s41598-025-95641-3","article-title":"An African swine fever vaccine-like variant with multiple gene deletions caused reproductive failure in a Vietnamese breeding herd","volume":"15","author":"Nguyen","year":"2025","journal-title":"Sci. Rep."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1038\/s41541-025-01099-9","article-title":"African swine fever virus vaccine strain Asfv-G-\u2206I177l reverts to virulence and negatively affects reproductive performance","volume":"10","author":"Olasz","year":"2025","journal-title":"npj Vaccines"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1002\/jcb.30143","article-title":"Biochemical strategies of E3 ubiquitin ligases target viruses in critical diseases","volume":"123","author":"Dubey","year":"2022","journal-title":"J. Cell. Biochem."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1089\/vim.2024.0068","article-title":"Involvement of E3 Ubiquitin Ligases in Viral Infections of the Human Host","volume":"37","author":"Verma","year":"2024","journal-title":"Viral Immunol."},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Bialek, W., Collawn, J.F., and Bartoszewski, R. (2023). Ubiquitin-Dependent and Independent Proteasomal Degradation in Host-Pathogen Interactions. Molecules, 28.","DOI":"10.3390\/molecules28186740"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1186\/s13578-022-00870-y","article-title":"Current methodologies in protein ubiquitination characterization: From ubiquitinated protein to ubiquitin chain architecture","volume":"12","author":"Sun","year":"2022","journal-title":"Cell Biosci."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.semcancer.2020.05.002","article-title":"RBR E3 ubiquitin ligases in tumorigenesis","volume":"67","author":"Wang","year":"2020","journal-title":"Semin. Cancer Biol."},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Toma-Fukai, S., and Shimizu, T. (2021). Structural Diversity of Ubiquitin E3 Ligase. Molecules, 26.","DOI":"10.3390\/molecules26216682"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1007\/s10637-020-00894-6","article-title":"The structure and regulation of the E3 ubiquitin ligase HUWE1 and its biological functions in cancer","volume":"38","author":"Gong","year":"2020","journal-title":"Investig. New Drugs"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"194979","DOI":"10.1016\/j.bbagrm.2023.194979","article-title":"Ubiquitination and deubiquitination: Implications on cancer therapy","volume":"1866","author":"Dagar","year":"2023","journal-title":"Biochim. Biophys. Acta Gene Regul. Mech."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s11658-020-00245-6","article-title":"Beyond K48 and K63: Non-canonical protein ubiquitination","volume":"26","author":"Tracz","year":"2021","journal-title":"Cell. Mol. Biol. Lett."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1146\/annurev-biochem-060815-014922","article-title":"Ubiquitin Ligases: Structure, Function, and Regulation","volume":"86","author":"Zheng","year":"2017","journal-title":"Annu. Rev. Biochem."},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Buneeva, O., and Medvedev, A. (2022). Atypical Ubiquitination and Parkinson\u2019s Disease. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23073705"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"203","DOI":"10.24976\/Discov.Med.202537193.18","article-title":"The Ubiquitin Code in Disease Pathogenesis and Progression: Composition, Characteristics and its Potential as a Therapeutic Target","volume":"37","author":"Lee","year":"2025","journal-title":"Discov. Med."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1038\/s41421-020-00237-y","article-title":"Emerging functions of branched ubiquitin chains","volume":"7","author":"French","year":"2021","journal-title":"Cell Discov."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"759","DOI":"10.1016\/j.tibs.2022.04.003","article-title":"Assembly and function of branched ubiquitin chains","volume":"47","author":"Kolla","year":"2022","journal-title":"Trends Biochem. Sci."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1038\/s41418-020-00648-0","article-title":"Ubiquitin signaling in cell cycle control and tumorigenesis","volume":"28","author":"Dang","year":"2021","journal-title":"Cell Death Differ."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1002\/JLB.4RU0620-397RR","article-title":"K27-linked noncanonic ubiquitination in immune regulation","volume":"111","author":"Zhou","year":"2022","journal-title":"J. Leukoc. Biol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1111\/nph.20224","article-title":"The Arabidopsis E3 ubiquitin ligase DOA10A promotes localization of abscisic acid (ABA) receptors to the membrane through mono-ubiquitination in ABA signaling","volume":"245","author":"Liu","year":"2025","journal-title":"New Phytol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1007\/978-981-15-3266-5_13","article-title":"Regulation of Cancer Immune Checkpoint: Mono- and Poly-Ubiquitination: Tags for Fate","volume":"1248","author":"Yao","year":"2020","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"195033","DOI":"10.1016\/j.bbagrm.2024.195033","article-title":"To Ub or not to Ub: The epic dilemma of histones that regulate gene expression and epigenetic cross-talk","volume":"1867","author":"Dasgupta","year":"2024","journal-title":"Biochim. Biophys. Acta Gene Regul. Mech."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1348","DOI":"10.3724\/abbs.2023149","article-title":"Ubiquitination in the regulation of autophagy","volume":"55","author":"Cen","year":"2023","journal-title":"Acta Biochim. Biophys. Sin."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"2165","DOI":"10.1007\/s00018-016-2191-4","article-title":"Poly-ubiquitination in TNFR1-mediated necroptosis","volume":"73","author":"Dondelinger","year":"2016","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"e00322-19","DOI":"10.1128\/JVI.00322-19","article-title":"Newcastle Disease Virus V Protein Degrades Mitochondrial Antiviral Signaling Protein To Inhibit Host Type I Interferon Production via E3 Ubiquitin Ligase RNF5","volume":"93","author":"Sun","year":"2019","journal-title":"J. Virol."},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"Kong, Z., Yin, H., Wang, F., Liu, Z., Luan, X., Sun, L., Liu, W., and Shang, Y. (2022). Pseudorabies virus tegument protein UL13 recruits RNF5 to inhibit STING-mediated antiviral immunity. PLoS Pathog., 18.","DOI":"10.1371\/journal.ppat.1010544"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"109878","DOI":"10.1016\/j.virol.2023.109878","article-title":"Innate immune escape and adaptive immune evasion of African swine fever virus: A review","volume":"587","author":"Niu","year":"2023","journal-title":"Virology"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"110473","DOI":"10.1016\/j.vetmic.2025.110473","article-title":"S5092 inhibit ASFV infection by targeting the pS273R protease activity in vitro","volume":"304","author":"Liu","year":"2025","journal-title":"Vet. Microbiol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"2482697","DOI":"10.1080\/22221751.2025.2482697","article-title":"Thonningianin A disrupts pA104R-DNA binding and inhibits African swine fever virus replication","volume":"14","author":"Li","year":"2025","journal-title":"Emerg. Microbes Infect."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1146\/annurev-biochem-061516-044813","article-title":"Cyclic GMP-AMP as an Endogenous Second Messenger in Innate Immune Signaling by Cytosolic DNA","volume":"86","author":"Kato","year":"2017","journal-title":"Annu. Rev. Biochem."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1038\/nature12306","article-title":"CGAS produces a 2\u2032-5\u2032-linked cyclic dinucleotide second messenger that activates STING","volume":"498","author":"Ablasser","year":"2013","journal-title":"Nature"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"1647","DOI":"10.1038\/s12276-021-00691-y","article-title":"Regulation of antiviral innate immune signaling and viral evasion following viral genome sensing","volume":"53","author":"Chathuranga","year":"2021","journal-title":"Exp. Mol. Med."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"538","DOI":"10.1016\/j.immuni.2008.09.003","article-title":"The adaptor protein MITA links virus-sensing receptors to IRF3 transcription factor activation","volume":"29","author":"Zhong","year":"2008","journal-title":"Immunity"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"2525","DOI":"10.1007\/s00018-017-2520-2","article-title":"Advances in anti-viral immune defence: Revealing the importance of the IFN JAK\/STAT pathway","volume":"74","author":"Raftery","year":"2017","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_40","doi-asserted-by":"crossref","unstructured":"Fleming, S.B. (2016). Viral Inhibition of the IFN-Induced JAK\/STAT Signalling Pathway: Development of Live Attenuated Vaccines by Mutation of Viral-Encoded IFN-Antagonists. Vaccines, 4.","DOI":"10.3390\/vaccines4030023"},{"key":"ref_41","doi-asserted-by":"crossref","unstructured":"Hu, Q., Bian, Q., Rong, D., Wang, L., Song, J., Huang, H.S., Zeng, J., Mei, J., and Wang, P.Y. (2023). JAK\/STAT pathway: Extracellular signals, diseases, immunity, and therapeutic regimens. Front. Bioeng. Biotechnol., 11.","DOI":"10.3389\/fbioe.2023.1110765"},{"key":"ref_42","doi-asserted-by":"crossref","unstructured":"Ran, Y., Li, D., Xiong, M.G., Liu, H.N., Feng, T., Shi, Z.W., Li, Y.H., Wu, H.N., Wang, S.Y., and Zheng, H.X. (2022). African swine fever virus I267L acts as an important virulence factor by inhibiting RNA polymerase III-RIG-I-mediated innate immunity. PLoS Pathog., 18.","DOI":"10.1371\/journal.ppat.1010270"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"147383","DOI":"10.1016\/j.ijbiomac.2025.147383","article-title":"African swine fever virus-encoded pE248R protein inhibits interferon production via blocking RIG-I-mediated antiviral signaling","volume":"327","author":"Zhao","year":"2025","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"110669","DOI":"10.1016\/j.jbc.2025.110669","article-title":"African swine fever virus pMGF505-9R enhances RIG-I-like receptor signaling by promoting RING finger protein 125 autoubiquitination","volume":"301","author":"Zhao","year":"2025","journal-title":"J. Biol. Chem."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"111066","DOI":"10.1016\/j.vetmic.2026.111066","article-title":"ASFV early protein p30 suppresses antiviral type I IFN induction by targeting TRIM21 and RIG-I like receptor signaling adaptor MAVS","volume":"319","author":"Zhang","year":"2026","journal-title":"Vet. Microbiol."},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Li, Y., Huang, L., Li, H., Zhu, Y., Yu, Z., Zheng, X., Weng, C., and Feng, W.H. (2024). ASFV pA151R negatively regulates type I IFN production via degrading E3 ligase TRAF6. Front. Immunol., 15.","DOI":"10.3389\/fimmu.2024.1339510"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"2754","DOI":"10.4049\/jimmunol.2100320","article-title":"African Swine Fever Virus pI215L Negatively Regulates cGAS-STING Signaling Pathway through Recruiting RNF138 to Inhibit K63-Linked Ubiquitination of TBK1","volume":"207","author":"Huang","year":"2021","journal-title":"J. Immunol."},{"key":"ref_48","doi-asserted-by":"crossref","unstructured":"Wang, Y., Cui, S., Xin, T., Wang, X., Yu, H., Chen, S., Jiang, Y., Gao, X., Jiang, Y., and Guo, X. (2021). African Swine Fever Virus MGF360-14L Negatively Regulates Type I Interferon Signaling by Targeting IRF3. Front. Cell. Infect. Microbiol., 11.","DOI":"10.3389\/fcimb.2021.818969"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"e0060623","DOI":"10.1128\/mbio.00606-23","article-title":"African swine fever virus MGF-360-10L is a novel and crucial virulence factor that mediates ubiquitination and degradation of JAK1 by recruiting the E3 ubiquitin ligase HERC5","volume":"14","author":"Li","year":"2023","journal-title":"mBio"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"101190","DOI":"10.1016\/j.jbc.2021.101190","article-title":"African swine fever virus protein MGF-505-7R promotes virulence and pathogenesis by inhibiting JAK1- and JAK2-mediated signaling","volume":"297","author":"Li","year":"2021","journal-title":"J. Biol. Chem."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"e0194222","DOI":"10.1128\/jvi.01942-22","article-title":"African Swine Fever Virus Cysteine Protease pS273R Inhibits Type I Interferon Signaling by Mediating STAT2 Degradation","volume":"97","author":"Li","year":"2023","journal-title":"J. Virol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1038\/s42003-026-09681-0","article-title":"African swine fever virus\u2013encoded protein MGF 505\u20133R impairs innate immunity via ubiquitin\u2013mediated degradation of MyD88","volume":"9","author":"Liu","year":"2026","journal-title":"Commun. Biol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"e0208024","DOI":"10.1128\/jvi.02080-24","article-title":"African swine fever virus I177L induces host inflammatory responses by facilitating the TRAF6-TAK1 axis and NLRP3 inflammasome assembly","volume":"99","author":"Wu","year":"2025","journal-title":"J. Virol."},{"key":"ref_54","doi-asserted-by":"crossref","unstructured":"Lu, Z., Luo, R., Lan, J., Chen, S., Qiu, H.J., Wang, T., and Sun, Y. (2024). The MGF300-2R Protein of African Swine Fever Virus Promotes IKK\u03b2 Ubiquitination by Recruiting the E3 Ubiquitin Ligase TRIM21. Viruses, 16.","DOI":"10.3390\/v16060949"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1186\/s12964-025-02381-y","article-title":"African swine fever virus A179L inhibits interferon induced transmembrane protein 1 activation of NF-\u03baB pathway","volume":"23","author":"Sun","year":"2025","journal-title":"Cell Commun. Signal."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"2333381","DOI":"10.1080\/22221751.2024.2333381","article-title":"The African swine fever virus MGF300-4L protein is associated with viral pathogenicity by promoting the autophagic degradation of IKK\u03b2 and increasing the stability of I\u03baB\u03b1","volume":"13","author":"Wang","year":"2024","journal-title":"Emerg. Microbes Infect."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"199198","DOI":"10.1016\/j.virusres.2023.199198","article-title":"African swine fever virus MGF360-9L promotes viral replication by degrading the host protein HAX1","volume":"336","author":"Yang","year":"2023","journal-title":"Virus Res."},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Wen, Y., Duan, X., Ren, J., Zhang, J., Guan, G., Ru, Y., Li, D., and Zheng, H. (2024). African Swine Fever Virus I267L Is a Hemorrhage-Related Gene Based on Transcriptome Analysis. Microorganisms, 12.","DOI":"10.3390\/microorganisms12020400"},{"key":"ref_59","doi-asserted-by":"crossref","unstructured":"Zhang, Y., Ke, J., Zhang, J., Yue, H., Chen, T., Li, Q., Zhou, X., Qi, Y., Zhu, R., and Wang, S. (2021). I267L Is Neither the Virulence- Nor the Replication-Related Gene of African Swine Fever Virus and Its Deletant Is an Ideal Fluorescent-Tagged Virulence Strain. Viruses, 14.","DOI":"10.3390\/v14010053"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"7308","DOI":"10.1038\/s41467-023-42982-0","article-title":"The E3 ligase Riplet promotes RIG-I signaling independent of RIG-I oligomerization","volume":"14","author":"Wang","year":"2023","journal-title":"Nat. Commun."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"496","DOI":"10.1016\/j.chom.2010.11.008","article-title":"The ubiquitin ligase Riplet is essential for RIG-I-dependent innate immune responses to RNA virus infection","volume":"8","author":"Oshiumi","year":"2010","journal-title":"Cell Host Microbe"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"840","DOI":"10.1111\/imcb.12284","article-title":"RIPLET, and not TRIM25, is required for endogenous RIG-I-dependent antiviral responses","volume":"97","author":"Hayman","year":"2019","journal-title":"Immunol. Cell Biol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"e0052622","DOI":"10.1128\/jvi.00526-22","article-title":"Riplet Binds the Zinc Finger Antiviral Protein (ZAP) and Augments ZAP-Mediated Restriction of HIV-1","volume":"96","author":"Buckmaster","year":"2022","journal-title":"J. Virol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1007\/s12104-019-09895-w","article-title":"Backbone (1)H, (13)C, and (15)N resonance assignments of the PRY-SPRY domain of RNF135","volume":"13","author":"Zhang","year":"2019","journal-title":"Biomol. NMR Assign."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"18621","DOI":"10.1074\/jbc.M801451200","article-title":"Regulation of IkappaB kinase-related kinases and antiviral responses by tumor suppressor CYLD","volume":"283","author":"Zhang","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1038\/cr.2013.170","article-title":"USP3 inhibits type I interferon signaling by deubiquitinating RIG-I-like receptors","volume":"24","author":"Cui","year":"2014","journal-title":"Cell Res."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1074\/jbc.M804259200","article-title":"Riplet\/RNF135, a RING finger protein, ubiquitinates RIG-I to promote interferon-beta induction during the early phase of viral infection","volume":"284","author":"Oshiumi","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"12290","DOI":"10.1128\/JVI.01333-09","article-title":"The African swine fever virus virion membrane protein pE248R is required for virus infectivity and an early postentry event","volume":"83","author":"Nogal","year":"2009","journal-title":"J. Virol."},{"key":"ref_69","doi-asserted-by":"crossref","unstructured":"Urquiza, J., Cuesta-Geijo, M.\u00c1., Garc\u00eda-Dorival, I., Fern\u00e1ndez, \u00d3., Del Puerto, A., D\u00edaz, J.F., and Alonso, C. (2024). Identification of a Potential Entry-Fusion Complex Based on Sequence Homology of African Swine Fever and Vaccinia Virus. Viruses, 16.","DOI":"10.3390\/v16030349"},{"key":"ref_70","doi-asserted-by":"crossref","unstructured":"Cuesta-Geijo, M.\u00c1., Garc\u00eda-Dorival, I., Del Puerto, A., Urquiza, J., Galindo, I., Barrado-Gil, L., Lasala, F., Cayuela, A., Sorzano, C.O.S., and Gil, C. (2022). New insights into the role of endosomal proteins for African swine fever virus infection. PLoS Pathog., 18.","DOI":"10.1371\/journal.ppat.1009784"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"e1588","DOI":"10.1002\/wrna.1588","article-title":"TRIM25 and its emerging RNA-binding roles in antiviral defense","volume":"11","author":"Choudhury","year":"2020","journal-title":"Wiley Interdiscip. Rev. RNA"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"188954","DOI":"10.1016\/j.bbcan.2023.188954","article-title":"The role of TRIM25 in the occurrence and development of cancers and inflammatory diseases","volume":"1878","author":"Zaersabet","year":"2023","journal-title":"Biochim. Biophys. Acta Rev. Cancer"},{"key":"ref_73","doi-asserted-by":"crossref","unstructured":"Choudhury, N.R., Heikel, G., Trubitsyna, M., Kubik, P., Nowak, J.S., Webb, S., Granneman, S., Spanos, C., Rappsilber, J., and Castello, A. (2017). RNA-binding activity of TRIM25 is mediated by its PRY\/SPRY domain and is required for ubiquitination. BMC Biol., 15.","DOI":"10.1186\/s12915-017-0444-9"},{"key":"ref_74","doi-asserted-by":"crossref","unstructured":"Liu, Q., Peng, S., Wei, J., and Xie, Z. (2025). The Function of TRIM25 in Antiviral Defense and Viral Immune Evasion. Viruses, 17.","DOI":"10.3390\/v17050735"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"1315","DOI":"10.1016\/j.celrep.2016.06.070","article-title":"Mechanism of TRIM25 Catalytic Activation in the Antiviral RIG-I Pathway","volume":"16","author":"Sanchez","year":"2016","journal-title":"Cell Rep."},{"key":"ref_76","doi-asserted-by":"crossref","unstructured":"Hakobyan, S., Bayramyan, N., Karalyan, Z., Izmailyan, R., Avetisyan, A., Poghosyan, A., Arakelova, E., Vardanyan, T., and Avagyan, H. (2025). The Involvement of MGF505 Genes in the Long-Term Persistence of the African Swine Fever Virus in Gastropods. Viruses, 17.","DOI":"10.3390\/v17060824"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"e161935","DOI":"10.1172\/JCI161935","article-title":"Posttranslational ISGylation of NLRP3 by HERC enzymes facilitates inflammasome activation in models of inflammation","volume":"133","author":"Qin","year":"2023","journal-title":"J. Clin. Investig."},{"key":"ref_78","doi-asserted-by":"crossref","unstructured":"Huang, L., Li, J., Zheng, J., Li, D., and Weng, C. (2022). Multifunctional pMGF505-7R Is a Key Virulence-Related Factor of African Swine Fever Virus. Front. Microbiol., 13.","DOI":"10.3389\/fmicb.2022.852431"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"e0194322","DOI":"10.1128\/jvi.01943-22","article-title":"CP204L Is a Multifunctional Protein of African Swine Fever Virus That Interacts with the VPS39 Subunit of the Homotypic Fusion and Vacuole Protein Sorting Complex and Promotes Lysosome Clustering","volume":"97","author":"Dolata","year":"2023","journal-title":"J. Virol."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"3275","DOI":"10.1016\/j.febslet.2008.08.031","article-title":"African swine fever virus protein p30 interaction with heterogeneous nuclear ribonucleoprotein K (hnRNP-K) during infection","volume":"582","author":"Hernaez","year":"2008","journal-title":"FEBS Lett."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"1449","DOI":"10.1038\/s41598-018-19626-1","article-title":"Efficient inhibition of African swine fever virus replication by CRISPR\/Cas9 targeting of the viral p30 gene (CP204L)","volume":"8","author":"Petersen","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"e00321-18","DOI":"10.1128\/JVI.00321-18","article-title":"TRIM21 Promotes Innate Immune Response to RNA Viral Infection through Lys27-Linked Polyubiquitination of MAVS","volume":"92","author":"Xue","year":"2018","journal-title":"J. Virol."},{"key":"ref_83","doi-asserted-by":"crossref","unstructured":"Ramirez-Medina, E., Vuono, E., Pruitt, S., Rai, A., Espinoza, N., Valladares, A., Spinard, E., Silva, E., Velazquez-Salinas, L., and Gladue, D.P. (2022). ASFV Gene A151R Is Involved in the Process of Virulence in Domestic Swine. Viruses, 14.","DOI":"10.3390\/v14081834"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1016\/j.bbrc.2020.08.011","article-title":"Structure basis of non-structural protein pA151R from African Swine Fever Virus","volume":"532","author":"Huang","year":"2020","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1186\/s12935-020-01517-z","article-title":"The relationship between TRAF6 and tumors","volume":"20","author":"Li","year":"2020","journal-title":"Cancer Cell Int."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1002\/cbic.201800436","article-title":"Binding and Enhanced Binding between Key Immunity Proteins TRAF6 and TIFA","volume":"20","author":"Huang","year":"2019","journal-title":"Chembiochem"},{"key":"ref_87","doi-asserted-by":"crossref","unstructured":"Fang, R., Jiang, Q., Zhou, X., Wang, C., Guan, Y., Tao, J., Xi, J., Feng, J.M., and Jiang, Z. (2017). MAVS activates TBK1 and IKK\u03b5 through TRAFs in NEMO dependent and independent manner. PLoS Pathog., 13.","DOI":"10.1371\/journal.ppat.1006720"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"2781","DOI":"10.1080\/15548627.2022.2047384","article-title":"TRAF6 autophagic degradation by avibirnavirus VP3 inhibits antiviral innate immunity via blocking NFKB\/NF-\u03baB activation","volume":"18","author":"Deng","year":"2022","journal-title":"Autophagy"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.virol.2022.01.001","article-title":"Influenza D virus Matrix protein 1 restricts the type I interferon response by degrading TRAF6","volume":"568","author":"Chen","year":"2022","journal-title":"Virology"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1016\/j.ijbiomac.2022.07.132","article-title":"The matrix protein of Newcastle disease virus inhibits inflammatory response through IRAK4\/TRAF6\/TAK1\/NF-\u03baB signaling pathway","volume":"218","author":"Duan","year":"2022","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"3471","DOI":"10.1038\/s41598-018-21872-2","article-title":"African swine fever virus encodes for an E2-ubiquitin conjugating enzyme that is mono- and di-ubiquitinated and required for viral replication cycle","volume":"8","author":"Freitas","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_92","doi-asserted-by":"crossref","unstructured":"Riera, E., Garc\u00eda-Belmonte, R., Madrid, R., P\u00e9rez-N\u00fa\u00f1ez, D., and Revilla, Y. (2022). African swine fever virus ubiquitin-conjugating enzyme pI215L inhibits IFN-I signaling pathway through STAT2 degradation. Front. Microbiol., 13.","DOI":"10.3389\/fmicb.2022.1081035"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"e0094422","DOI":"10.1128\/jvi.00944-22","article-title":"African Swine Fever Virus pI215L Inhibits Type I Interferon Signaling by Targeting Interferon Regulatory Factor 9 for Autophagic Degradation","volume":"96","author":"Li","year":"2022","journal-title":"J. Virol."},{"key":"ref_94","doi-asserted-by":"crossref","unstructured":"Gao, Y., Jiang, X., Yang, X., Zhang, K., Jiang, P., and Bai, J. (2023). Novel Epitope Mapping of African Swine Fever Virus pI215L Protein Using Monoclonal Antibodies. Viruses, 15.","DOI":"10.3390\/v15102081"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"1342","DOI":"10.1038\/ni.3588","article-title":"E3 ubiquitin ligase RNF128 promotes innate antiviral immunity through K63-linked ubiquitination of TBK1","volume":"17","author":"Song","year":"2016","journal-title":"Nat. Immunol."},{"key":"ref_96","doi-asserted-by":"crossref","unstructured":"Wang, L., Li, Y., Zhang, X., Madera, R., Pantua, H., Craig, A., Muro, N., Li, D., Retallick, J., and Ferreyra, F.M. (2025). Specific Detection of African Swine Fever Virus Variants: Novel Quadplex Real-Time PCR Assay with Internal Control. Microorganisms, 13.","DOI":"10.20944\/preprints202502.0813.v1"},{"key":"ref_97","doi-asserted-by":"crossref","unstructured":"Lin, C., Zhang, C., Chen, N., Meurens, F., Zhu, J., and Zheng, W. (2024). How Does African Swine Fever Virus Evade the cGAS-STING Pathway?. Pathogens, 13.","DOI":"10.3390\/pathogens13110957"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"143159","DOI":"10.1016\/j.ijbiomac.2025.143159","article-title":"DNAJA3 interacts with ASFV MGF360-14L protein and reduces MGF360-14L antagonistic role on Beta interferon production","volume":"310","author":"Wang","year":"2025","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_99","doi-asserted-by":"crossref","unstructured":"Gao, Q., Yang, Y., Quan, W., Zheng, J., Luo, Y., Wang, H., Chen, X., Huang, Z., Chen, X., and Xu, R. (2021). The African Swine Fever Virus with MGF360 and MGF505 Deleted Reduces the Apoptosis of Porcine Alveolar Macrophages by Inhibiting the NF-\u03baB Signaling Pathway and Interleukin-1\u03b2. Vaccines, 9.","DOI":"10.3390\/vaccines9111371"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"e0189921","DOI":"10.1128\/jvi.01899-21","article-title":"Differential Effect of Deleting Members of African Swine Fever Virus Multigene Families 360 and 505 from the Genotype II Georgia 2007\/1 Isolate on Virus Replication, Virulence, and Induction of Protection","volume":"96","author":"Rathakrishnan","year":"2022","journal-title":"J. Virol."},{"key":"ref_101","doi-asserted-by":"crossref","unstructured":"Zheng, L., Yan, Z., Qi, X., Ren, J., Ma, Z., Liu, H., Zhang, Z., Li, D., Pei, J., and Xiao, S. (2025). The Deletion of the MGF360-10L\/505-7R Genes of African Swine Fever Virus Results in High Attenuation but No Protection Against Homologous Challenge in Pigs. Viruses, 17.","DOI":"10.3390\/v17020283"},{"key":"ref_102","doi-asserted-by":"crossref","unstructured":"Fiori, M.S., Ferretti, L., Di Nardo, A., Zhao, L., Zinellu, S., Angioi, P.P., Floris, M., Sechi, A.M., Denti, S., and Cappai, S. (2022). A Naturally Occurring Microhomology-Mediated Deletion of Three Genes in African Swine Fever Virus Isolated from Two Sardinian Wild Boars. Viruses, 14.","DOI":"10.3390\/v14112524"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"114135","DOI":"10.1016\/j.celrep.2024.114135","article-title":"ISGylation by HERCs facilitates STING activation","volume":"43","author":"Qin","year":"2024","journal-title":"Cell Rep."},{"key":"ref_104","doi-asserted-by":"crossref","unstructured":"Bosch-Cam\u00f3s, L., L\u00f3pez, E., Collado, J., Navas, M.J., Blanco-Fuertes, M., Pina-Pedrero, S., Accensi, F., Salas, M.L., Mundt, E., and Nikolin, V. (2021). M448R and MGF505-7R: Two African Swine Fever Virus Antigens Commonly Recognized by ASFV-Specific T-Cells and with Protective Potential. Vaccines, 9.","DOI":"10.3390\/vaccines9050508"},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1016\/j.virusres.2012.10.013","article-title":"Identification and utility of innate immune system evasion mechanisms of ASFV","volume":"173","author":"Correia","year":"2013","journal-title":"Virus Res."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"198931","DOI":"10.1016\/j.virusres.2022.198931","article-title":"African swine fever virus MGF505-7R protein interacted with IRF7and TBK1 to inhibit type I interferon production","volume":"322","author":"Yang","year":"2022","journal-title":"Virus Res."},{"key":"ref_107","doi-asserted-by":"crossref","unstructured":"Li, J., Song, J., Kang, L., Huang, L., Zhou, S., Hu, L., Zheng, J., Li, C., Zhang, X., and He, X. (2021). PMGF505-7R determines pathogenicity of African swine fever virus infection by inhibiting IL-1\u03b2 and type I IFN production. PLoS Pathog., 17.","DOI":"10.1371\/journal.ppat.1009733"},{"key":"ref_108","doi-asserted-by":"crossref","unstructured":"Liu, X., Ao, D., Jiang, S., Xia, N., Xu, Y., Shao, Q., Luo, J., Wang, H., Zheng, W., and Chen, N. (2021). African Swine Fever Virus A528R Inhibits TLR8 Mediated NF-\u03baB Activity by Targeting p65 Activation and Nuclear Translocation. Viruses, 13.","DOI":"10.3390\/v13102046"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"e0022823","DOI":"10.1128\/jvi.00228-23","article-title":"Combinational Deletions of MGF110-9L and MGF505-7R Genes from the African Swine Fever Virus Inhibit TBK1 Degradation by an Autophagy Activator PIK3C2B To Promote Type I Interferon Production","volume":"97","author":"Zhu","year":"2023","journal-title":"J. Virol."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"e0032922","DOI":"10.1128\/jvi.00329-22","article-title":"Combinational Deletions of MGF360-9L and MGF505-7R Attenuated Highly Virulent African Swine Fever Virus and Conferred Protection against Homologous Challenge","volume":"96","author":"Ding","year":"2022","journal-title":"J. Virol."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"1458","DOI":"10.1016\/j.celrep.2015.04.049","article-title":"Downregulation of the Ubiquitin Ligase RNF125 Underlies Resistance of Melanoma Cells to BRAF Inhibitors via JAK1 Deregulation","volume":"11","author":"Kim","year":"2015","journal-title":"Cell Rep."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"104844","DOI":"10.1016\/j.jbc.2023.104844","article-title":"African swine fever virus pS273R antagonizes stress granule formation by cleaving the nucleating protein G3BP1 to facilitate viral replication","volume":"299","author":"Li","year":"2023","journal-title":"J. Biol. Chem."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"780","DOI":"10.1074\/jbc.M006844200","article-title":"African swine fever virus protease, a new viral member of the SUMO-1-specific protease family","volume":"276","author":"Alejo","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"116055","DOI":"10.1016\/j.bmc.2021.116055","article-title":"Small molecule inhibitor E-64 exhibiting the activity against African swine fever virus pS273R","volume":"35","author":"Liu","year":"2021","journal-title":"Bioorganic Med. Chem."},{"key":"ref_115","doi-asserted-by":"crossref","unstructured":"Han, H., Zhang, D., Hao, W., Liu, A., Xia, N., Cui, M., Luo, J., Jiang, S., Zheng, W., and Chen, N. (2025). Parallel and Visual Detections of ASFV by CRISPR-Cas12a and CRISPR-Cas13a Systems Targeting the Viral S273R Gene. Animals, 15.","DOI":"10.3390\/ani15131902"},{"key":"ref_116","doi-asserted-by":"crossref","unstructured":"Fenster, J.A., Azzinaro, P.A., Dinhobl, M., Borca, M.V., Spinard, E., and Gladue, D.P. (2024). African Swine Fever Virus Protein-Protein Interaction Prediction. Viruses, 16.","DOI":"10.3390\/v16071170"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"e0222524","DOI":"10.1128\/jvi.02225-24","article-title":"The S273R protein of African swine fever virus antagonizes the canonical NF-\u03baB signaling pathway by I\u03baB\u03b1","volume":"99","author":"Ren","year":"2025","journal-title":"J. Virol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"101480","DOI":"10.1016\/j.jbc.2021.101480","article-title":"African swine fever virus cysteine protease pS273R inhibits pyroptosis by noncanonically cleaving gasdermin D","volume":"298","author":"Zhao","year":"2022","journal-title":"J. Biol. Chem."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"36179","DOI":"10.1038\/srep36179","article-title":"Global functional profiling of human ubiquitome identifies E3 ubiquitin ligase DCST1 as a novel negative regulator of Type-I interferon signaling","volume":"6","author":"Nair","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"e66313","DOI":"10.7554\/eLife.66313","article-title":"Evolutionarily conserved sperm factors, DCST1 and DCST2, are required for gamete fusion","volume":"10","author":"Inoue","year":"2021","journal-title":"Elife"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1002\/wsbm.1331","article-title":"Signaling via the NF\u03baB system","volume":"8","author":"Mitchell","year":"2016","journal-title":"Wiley Interdiscip. Rev. Syst. Biol. Med."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1111\/2049-632X.12210","article-title":"The role of the IKK complex in viral infections","volume":"72","author":"Amaya","year":"2014","journal-title":"Pathog. Dis."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"1601","DOI":"10.1098\/rstb.1999.0504","article-title":"Control of NF-kappa B transcriptional activation by signal induced proteolysis of I kappa B alpha","volume":"354","author":"Hay","year":"1999","journal-title":"Philos. Trans. R. Soc. Lond. B Biol. Sci."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1016\/j.gendis.2020.06.005","article-title":"The Nuclear Factor Kappa B (NF-kB) signaling in cancer development and immune diseases","volume":"8","author":"Zinatizadeh","year":"2021","journal-title":"Genes Dis."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/j.virs.2022.03.006","article-title":"Regulation of antiviral immune response by African swine fever virus (ASFV)","volume":"37","author":"Zheng","year":"2022","journal-title":"Virol. Sin."},{"key":"ref_126","doi-asserted-by":"crossref","unstructured":"Kesika, P., Thangaleela, S., Sisubalan, N., Radha, A., Sivamaruthi, B.S., and Chaiyasut, C. (2024). The Role of the Nuclear Factor-Kappa B (NF-\u03baB) Pathway in SARS-CoV-2 Infection. Pathogens, 13.","DOI":"10.3390\/pathogens13020164"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"e0342324","DOI":"10.1128\/spectrum.03423-24","article-title":"African swine fever virus MGF505-3R facilitates ferroptosis to restrict TBK1-IRF3 pathway","volume":"13","author":"Niu","year":"2025","journal-title":"Microbiol. Spectr."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"6048","DOI":"10.1128\/JVI.00554-15","article-title":"African Swine Fever Virus Georgia Isolate Harboring Deletions of MGF360 and MGF505 Genes Is Attenuated in Swine and Confers Protection against Challenge with Virulent Parental Virus","volume":"89","author":"Holinka","year":"2015","journal-title":"J. Virol."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1186\/s44149-022-00046-8","article-title":"African swine fever virus MGF505-3R inhibits cGAS-STING-mediated IFN-\u03b2 pathway activation by degrading TBK1","volume":"2","author":"Cheng","year":"2022","journal-title":"Anim. Dis."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"2608396","DOI":"10.1080\/22221751.2025.2608396","article-title":"The deletion of the EP402R and MGF505\/360 genes attenuates a genotype I\/II recombinant ASFV but fails to confer complete protection against homologous or genotype II challenge in pigs","volume":"15","author":"Li","year":"2026","journal-title":"Emerg. Microbes Infect."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"474","DOI":"10.1016\/S0968-0004(02)02145-X","article-title":"A universal role for MyD88 in TLR\/IL-1R-mediated signaling","volume":"27","author":"Janssens","year":"2002","journal-title":"Trends Biochem. Sci."},{"key":"ref_132","doi-asserted-by":"crossref","unstructured":"Borca, M.V., Ramirez-Medina, E., Silva, E., Vuono, E., Rai, A., Pruitt, S., Espinoza, N., Velazquez-Salinas, L., Gay, C.G., and Gladue, D.P. (2021). ASFV-G-\u2206I177L as an Effective Oral Nasal Vaccine against the Eurasia Strain of Africa Swine Fever. Viruses, 13.","DOI":"10.3390\/v13050765"},{"key":"ref_133","doi-asserted-by":"crossref","unstructured":"Borca, M.V., Ramirez-Medina, E., Silva, E., Rai, A., Espinoza, N., Velazquez-Salinas, L., and Gladue, D.P. (2023). ASF Vaccine Candidate ASFV-G-\u2206I177L Does Not Exhibit Residual Virulence in Long-Term Clinical Studies. Pathogens, 12.","DOI":"10.3390\/pathogens12060805"},{"key":"ref_134","doi-asserted-by":"crossref","unstructured":"Shi, J., Liu, W., Zhang, M., Sun, J., and Xu, X. (2021). The A179L Gene of African Swine Fever Virus Suppresses Virus-Induced Apoptosis but Enhances Necroptosis. Viruses, 13.","DOI":"10.3390\/v13122490"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"e0110623","DOI":"10.1128\/jvi.01106-23","article-title":"Deletion of the gene for the African swine fever virus BCL-2 family member A179L increases virus uptake and apoptosis but decreases virus spread in macrophages and reduces virulence in pigs","volume":"97","author":"Reis","year":"2023","journal-title":"J. Virol."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1016\/j.virol.2008.01.050","article-title":"A179L, a viral Bcl-2 homologue, targets the core Bcl-2 apoptotic machinery and its upstream BH3 activators with selective binding restrictions for Bid and Noxa","volume":"375","author":"Galindo","year":"2008","journal-title":"Virology"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"e02228-16","DOI":"10.1128\/JVI.02228-16","article-title":"Structural Insight into African Swine Fever Virus A179L-Mediated Inhibition of Apoptosis","volume":"91","author":"Banjara","year":"2017","journal-title":"J. Virol."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"305","DOI":"10.2174\/15665240113130200007","article-title":"A179L, a new viral Bcl2 homolog targeting Beclin 1 autophagy related protein","volume":"13","author":"Hernaez","year":"2013","journal-title":"Curr. Mol. Med."},{"key":"ref_139","doi-asserted-by":"crossref","unstructured":"Yu, C., Liu, Q., Zhao, Z., Zhai, J., Xue, M., Tang, Y.D., Wang, C., and Zheng, C. (2023). The emerging roles of MARCH8 in viral infections: A double-edged Sword. PLoS Pathog., 19.","DOI":"10.1371\/journal.ppat.1011619"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"3642","DOI":"10.1111\/febs.16017","article-title":"MARCH8: The tie that binds to viruses","volume":"289","author":"Tada","year":"2022","journal-title":"FEBS J."},{"key":"ref_141","doi-asserted-by":"crossref","unstructured":"Wang, T., Luo, R., Zhang, J., Lu, Z., Li, L.F., Zheng, Y.H., Pan, L., Lan, J., Zhai, H., and Huang, S. (2023). The MGF300-2R protein of African swine fever virus is associated with viral pathogenicity by promoting the autophagic degradation of IKK\u03b1 and IKK\u03b2 through the recruitment of TOLLIP. PLoS Pathog., 19.","DOI":"10.1371\/journal.ppat.1011580"},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"e0093224","DOI":"10.1128\/jvi.00932-24","article-title":"Advances in African swine fever virus molecular biology and host interactions contributing to new tools for control","volume":"99","author":"Dixon","year":"2025","journal-title":"J. Virol."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"127172","DOI":"10.1016\/j.vaccine.2025.127172","article-title":"Safety and efficacy of a Vero-adapted live attenuated vaccine candidate for African swine fever","volume":"56","author":"Suh","year":"2025","journal-title":"Vaccine"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"2703","DOI":"10.1111\/tbed.14018","article-title":"The genetic variation landscape of African swine fever virus reveals frequent positive selection and adaptive flexibility","volume":"68","author":"Bao","year":"2021","journal-title":"Transbound. Emerg. Dis."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"2028","DOI":"10.1038\/sj.onc.1207389","article-title":"The many faces of beta-TrCP E3 ubiquitin ligases: Reflections in the magic mirror of cancer","volume":"23","author":"Fuchs","year":"2004","journal-title":"Oncogene"},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1042\/BST20150011","article-title":"Dual regulation of transcription factor Nrf2 by Keap1 and by the combined actions of \u03b2-TrCP and GSK-3","volume":"43","author":"Hayes","year":"2015","journal-title":"Biochem. Soc. Trans."},{"key":"ref_147","doi-asserted-by":"crossref","unstructured":"Mitchell, R.S., Katsura, C., Skasko, M.A., Fitzpatrick, K., Lau, D., Ruiz, A., Stephens, E.B., Margottin-Goguet, F., Benarous, R., and Guatelli, J.C. (2009). Vpu antagonizes BST-2-mediated restriction of HIV-1 release via beta-TrCP and endo-lysosomal trafficking. PLoS Pathog., 5.","DOI":"10.1371\/journal.ppat.1000450"},{"key":"ref_148","doi-asserted-by":"crossref","unstructured":"Mansur, D.S., Maluquer de Motes, C., Unterholzner, L., Sumner, R.P., Ferguson, B.J., Ren, H., Strnadova, P., Bowie, A.G., and Smith, G.L. (2013). Poxvirus targeting of E3 ligase \u03b2-TrCP by molecular mimicry: A mechanism to inhibit NF-\u03baB activation and promote immune evasion and virulence. PLoS Pathog., 9.","DOI":"10.1371\/journal.ppat.1003183"},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"104767","DOI":"10.1016\/j.jbc.2023.104767","article-title":"Deletions of MGF110-9L and MGF360-9L from African swine fever virus are highly attenuated in swine and confer protection against homologous challenge","volume":"299","author":"Li","year":"2023","journal-title":"J. Biol. Chem."},{"key":"ref_150","doi-asserted-by":"crossref","unstructured":"Yang, B., Zhang, D., Shi, X., Shen, C., Hao, Y., Zhang, T., Yang, J., Yuan, X., Chen, X., and Zhao, D. (2021). Construction, Identification and Analysis of the Interaction Network of African Swine Fever Virus MGF360-9L with Host Proteins. Viruses, 13.","DOI":"10.3390\/v13091804"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"e0233021","DOI":"10.1128\/mbio.02330-21","article-title":"MGF360-9L Is a Major Virulence Factor Associated with the African Swine Fever Virus by Antagonizing the JAK\/STAT Signaling Pathway","volume":"13","author":"Zhang","year":"2022","journal-title":"mBio"},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"1938","DOI":"10.1093\/hmg\/ddn091","article-title":"Identification of ZNF313\/RNF114 as a novel psoriasis susceptibility gene","volume":"17","author":"Capon","year":"2008","journal-title":"Hum. Mol. Genet."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"108746","DOI":"10.1016\/j.vetmic.2020.108746","article-title":"Proteasomal degradation of nonstructural protein 12 by RNF114 suppresses porcine reproductive and respiratory syndrome virus replication","volume":"246","author":"Bai","year":"2020","journal-title":"Vet. Microbiol."},{"key":"ref_154","doi-asserted-by":"crossref","unstructured":"Gupta, S., Yl\u00e4-Anttila, P., Callegari, S., Tsai, M.-H., Delecluse, H.-J., and Masucci, M.G. (2018). Herpesvirus deconjugases inhibit the IFN response by promoting TRIM25 autoubiquitination and functional inactivation of the RIG-I signalosome. PLoS Pathog., 14.","DOI":"10.1371\/journal.ppat.1006852"},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"3581","DOI":"10.1128\/JVI.02072-08","article-title":"Identification of TRIM23 as a cofactor involved in the regulation of NF-\u03baB by human cytomegalovirus","volume":"83","author":"Poole","year":"2009","journal-title":"J. Virol."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"e00898\u201325","DOI":"10.1128\/jvi.00898-25","article-title":"The vaccinia virus protein, C16, promotes the ubiquitylation and relocalization of the antiviral E3 ubiquitin-ligase, TRIM25","volume":"99","author":"Dong","year":"2025","journal-title":"J. Virol."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"12935","DOI":"10.1128\/JVI.01952-13","article-title":"Herpes simplex virus 1 E3 ubiquitin ligase ICP0 protein inhibits tumor necrosis factor alpha-induced NF-\u03baB activation by interacting with p65\/RelA and p50\/NF-\u03baB1","volume":"87","author":"Zhang","year":"2013","journal-title":"J. Virol."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"10802","DOI":"10.1128\/JVI.00063-10","article-title":"Herpes simplex virus immediate-early ICP0 protein inhibits Toll-like receptor 2-dependent inflammatory responses and NF-\u03baB signaling","volume":"84","author":"Murawski","year":"2010","journal-title":"J. Virol."},{"key":"ref_159","doi-asserted-by":"crossref","unstructured":"Cui, H., Zhang, Y., and Zhang, L. (2021). Progress on poxvirus E3 ubiquitin ligases and adaptor proteins. Front. Immunol., 12.","DOI":"10.3389\/fimmu.2021.740223"},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/j.immuni.2004.11.011","article-title":"The KSHV immediate-early transcription factor RTA encodes ubiquitin E3 ligase activity that targets IRF7 for proteosome-mediated degradation","volume":"22","author":"Yu","year":"2005","journal-title":"Immunity"}],"container-title":["Pathogens"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-0817\/15\/7\/716\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,7,8]],"date-time":"2026-07-08T13:09:00Z","timestamp":1783516140000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-0817\/15\/7\/716"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,7,7]]},"references-count":160,"journal-issue":{"issue":"7","published-online":{"date-parts":[[2026,7]]}},"alternative-id":["pathogens15070716"],"URL":"https:\/\/doi.org\/10.3390\/pathogens15070716","relation":{},"ISSN":["2076-0817"],"issn-type":[{"value":"2076-0817","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,7,7]]}}}