{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,20]],"date-time":"2026-08-20T16:38:49Z","timestamp":1787243929773,"version":"build-2736575974"},"reference-count":51,"publisher":"MDPI AG","issue":"9","license":[{"start":{"date-parts":[[2023,9,8]],"date-time":"2023-09-08T00:00:00Z","timestamp":1694131200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Science and Technology Innovation Project of Chinese Academy of Agricultural Sciences","award":["CAAS-ASTIP-2019-LVRI-06"],"award-info":[{"award-number":["CAAS-ASTIP-2019-LVRI-06"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Microorganisms"],"abstract":"<jats:p>Guanylate-binding proteins (GBPs) are highly expressed interferon-stimulated genes (ISGs) that play significant roles in protecting against invading pathogens. Although their functions in response to RNA viruses have been extensively investigated, there is limited information available regarding their role in DNA viruses, particularly poxviruses. Ectromelia virus (ECTV), a member of the orthopoxvirus genus, is a large double-stranded DNA virus closely related to the monkeypox virus and variola virus. It has been intensively studied as a highly effective model virus. According to the study, GBP2 overexpression suppresses ECTV replication in a dose-dependent manner, while GBP2 knockdown promotes ECTV infection. Additionally, it was discovered that GBP2 primarily functions through its N-terminal GTPase activity, and the inhibitory effect of GBP2 was disrupted in the GTP-binding-impaired mutant GBP2K51A. This study is the first to demonstrate the inhibitory effect of GBP2 on ECTV, and it offers insights into innovative antiviral strategies.<\/jats:p>","DOI":"10.3390\/microorganisms11092258","type":"journal-article","created":{"date-parts":[[2023,9,8]],"date-time":"2023-09-08T07:57:17Z","timestamp":1694159837000},"page":"2258","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["Guanylate-Binding Protein 2 Exerts GTPase-Dependent Anti-Ectromelia Virus Effect"],"prefix":"10.3390","volume":"11","author":[{"given":"Zhenzhen","family":"Gao","sequence":"first","affiliation":[{"name":"State Key Laboratory for Animal Disease Control and Prevention, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China"},{"name":"Ministry of Agriculture Key Laboratory of Veterinary Public Health, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China"},{"name":"Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zejing","family":"Meng","sequence":"additional","affiliation":[{"name":"School of Public Health, Lanzhou University, Lanzhou 730000, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiaobing","family":"He","sequence":"additional","affiliation":[{"name":"State Key Laboratory for Animal Disease Control and Prevention, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China"},{"name":"Ministry of Agriculture Key Laboratory of Veterinary Public Health, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China"},{"name":"Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Guohua","family":"Chen","sequence":"additional","affiliation":[{"name":"State Key Laboratory for Animal Disease Control and Prevention, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China"},{"name":"Ministry of Agriculture Key Laboratory of Veterinary Public Health, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China"},{"name":"Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yongxiang","family":"Fang","sequence":"additional","affiliation":[{"name":"State Key Laboratory for Animal Disease Control and Prevention, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China"},{"name":"Ministry of Agriculture Key Laboratory of Veterinary Public Health, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China"},{"name":"Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Huihui","family":"Tian","sequence":"additional","affiliation":[{"name":"State Key Laboratory for Animal Disease Control and Prevention, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China"},{"name":"Ministry of Agriculture Key Laboratory of Veterinary Public Health, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China"},{"name":"Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hui","family":"Zhang","sequence":"additional","affiliation":[{"name":"State Key Laboratory for Animal Disease Control and Prevention, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China"},{"name":"Ministry of Agriculture Key Laboratory of Veterinary Public Health, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China"},{"name":"Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhizhong","family":"Jing","sequence":"additional","affiliation":[{"name":"State Key Laboratory for Animal Disease Control and Prevention, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China"},{"name":"Ministry of Agriculture Key Laboratory of Veterinary Public Health, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China"},{"name":"Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China"},{"name":"School of Public Health, Lanzhou University, Lanzhou 730000, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,9,8]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Mavian, C., L\u00f3pez-Bueno, A., Mart\u00edn, R., Nitsche, A., and Alcam\u00ed, A. (2021). Comparative pathogenesis, genomics and phylogeography of mousepox. Viruses, 13.","DOI":"10.3390\/v13061146"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"636","DOI":"10.1016\/j.it.2004.10.002","article-title":"25 years since the eradication of smallpox: Why poxvirus research is still relevant","volume":"25","author":"Mahalingam","year":"2004","journal-title":"Trends Immunol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"e30406","DOI":"10.1097\/MD.0000000000030406","article-title":"Human monkeypox virus: An updated review","volume":"101","author":"Adnan","year":"2022","journal-title":"Medicine"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1016\/bs.ai.2015.10.001","article-title":"The pathogenesis and immunobiology of mousepox","volume":"129","author":"Sigal","year":"2016","journal-title":"Adv. Immunol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"1148","DOI":"10.1016\/j.immuni.2015.11.015","article-title":"Sequential activation of two pathogen-sensing pathways is required for type I interferon expression and resistance to an acute DNA virus infection","volume":"43","author":"Xu","year":"2015","journal-title":"Immunity"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.coviro.2014.03.006","article-title":"Interferon-stimulated genes: Roles in viral pathogenesis","volume":"6","author":"Schoggins","year":"2014","journal-title":"Curr. Opin. Virol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"494","DOI":"10.1093\/rheumatology\/keaa609","article-title":"Interferon-stimulated GTPases in autoimmune and inflammatory diseases: Promising role for the guanylate-binding protein (GBP) family","volume":"60","author":"Haque","year":"2021","journal-title":"Rheumatology"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1016\/j.chom.2012.09.007","article-title":"IFN-inducible GTPases in host cell defense","volume":"12","author":"Kim","year":"2012","journal-title":"Cell Host Microbe."},{"key":"ref_9","doi-asserted-by":"crossref","unstructured":"Kresse, A., Konermann, C., Degrandi, D., Beuter-Gunia, C., Wuerthner, J., Pfeffer, K., and Beer, S. (2008). Analyses of murine GBP homology clusters based on in silico, in vitro and in vivo studies. BMC Genom., 9.","DOI":"10.1186\/1471-2164-9-158"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"5826","DOI":"10.1111\/febs.15662","article-title":"Human guanylate binding proteins: Nanomachines orchestrating host defense","volume":"288","author":"Kutsch","year":"2021","journal-title":"FEBS J."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"155388","DOI":"10.1016\/j.cyto.2020.155388","article-title":"Tupaia guanylate-binding protein 1 interacts with vesicular stomatitis virus phosphoprotein and represses primary transcription of the viral genome","volume":"138","author":"Gu","year":"2021","journal-title":"Cytokine"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"e01564-20","DOI":"10.1128\/JVI.01564-20","article-title":"Identification of the interferon-inducible GTPase GBP1 as major restriction factor for the Hepatitis E virus","volume":"95","author":"Glitscher","year":"2021","journal-title":"J. Virol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1727","DOI":"10.1002\/hep.23195","article-title":"Antiviral effects of the interferon-induced protein guanylate binding protein 1 and its interaction with the hepatitis C virus NS5B protein","volume":"50","author":"Itsui","year":"2009","journal-title":"Hepatology"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"4412","DOI":"10.1128\/JVI.02718-15","article-title":"Guanylate-Binding Protein 1, an Interferon-Induced GTPase, Exerts an Antiviral Activity against Classical Swine Fever Virus Depending on Its GTPase Activity","volume":"90","author":"Li","year":"2016","journal-title":"J. Virol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"1213","DOI":"10.1007\/s00705-004-0489-2","article-title":"Inhibition of VSV and EMCV replication by the interferon-induced GTPase, mGBP-2: Differential requirement for wild-type GTP binding domain","volume":"150","author":"Carter","year":"2005","journal-title":"Arch. Virol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"8036","DOI":"10.1074\/jbc.RA120.013544","article-title":"Guanylate-binding protein 2 orchestrates innate immune responses against murine norovirus and is antagonized by the viral protein NS7","volume":"295","author":"Yu","year":"2020","journal-title":"J. Biol. Chem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"2092","DOI":"10.1016\/j.celrep.2019.04.063","article-title":"Guanylate-Binding Proteins 2 and 5 Exert Broad Antiviral Activity by Inhibiting Furin-Mediated Processing of Viral Envelope Proteins","volume":"27","author":"Braun","year":"2019","journal-title":"Cell. Rep."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1186\/s12929-021-00716-8","article-title":"When human guanylate-binding proteins meet viral infections","volume":"28","author":"Zhang","year":"2021","journal-title":"J. Biomed. Sci."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1189\/jlb.4MR0516-223R","article-title":"Interferon-inducible guanylate-binding proteins at the interface of cell-autonomous immunity and inflammasome activation","volume":"101","author":"Man","year":"2017","journal-title":"J. Leukoc. Biol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1002\/bip.22855","article-title":"Invited review: Mechanisms of GTP hydrolysis and conformational transitions in the dynamin superfamily","volume":"105","author":"Daumke","year":"2016","journal-title":"Biopolymers"},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Barz, B., Loschwitz, J., and Strodel, B. (2019). Large-scale, dynamin-like motions of the human guanylate binding protein 1 revealed by multi-resolution simulations. PLoS. Comput. Biol., 15.","DOI":"10.1101\/676981"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"e2022269118","DOI":"10.1073\/pnas.2022269118","article-title":"Structural basis for GTP-induced dimerization and antiviral function of guanylate-binding proteins","volume":"118","author":"Cui","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1007\/s00430-022-00736-7","article-title":"Functional cross-species conservation of guanylate-binding proteins in innate immunity","volume":"212","author":"Schelle","year":"2023","journal-title":"Med. Microbiol. Immunol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"2164","DOI":"10.1016\/j.jmb.2020.02.009","article-title":"The molecular mechanism of polymer formation of farnesylated human guanylate-binding protein 1","volume":"432","author":"Sistemich","year":"2020","journal-title":"J. Mol. Biol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1038\/nature04510","article-title":"How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP","volume":"440","author":"Ghosh","year":"2006","journal-title":"Nature"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1038\/nature09032","article-title":"G domain dimerization controls dynamin\u2019s assembly-stimulated GTPase activity","volume":"465","author":"Chappie","year":"2010","journal-title":"Nature"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"E5559","DOI":"10.1073\/pnas.1620959114","article-title":"Nucleotide-dependent farnesyl switch orchestrates polymerization and membrane binding of human guanylate-binding protein 1","volume":"114","author":"Shydlovskyi","year":"2017","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"e12791","DOI":"10.1111\/cmi.12791","article-title":"Mechanisms and functions of guanylate-binding proteins and related interferon-inducible GTPases: Roles in intracellular lysis of pathogens","volume":"19","author":"Ngo","year":"2017","journal-title":"Cell. Microbiol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1038\/ni.3118","article-title":"The transcription factor IRF1 and guanylate-binding proteins target activation of the AIM2 inflammasome by Francisella infection","volume":"16","author":"Man","year":"2015","journal-title":"Nat. Immunol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"4800","DOI":"10.3390\/v7082844","article-title":"Cloak and Dagger: Alternative Immune Evasion and Modulation Strategies of Poxviruses","volume":"7","author":"Bidgood","year":"2015","journal-title":"Viruses"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"5440","DOI":"10.1038\/s41467-018-07772-z","article-title":"A virus-encoded type I interferon decoy receptor enables evasion of host immunity through cell-surface binding","volume":"9","author":"Montanuy","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1084\/jem.20071854","article-title":"The orthopoxvirus type I IFN binding protein is essential for virulence and an effective target for vaccination","volume":"205","author":"Xu","year":"2008","journal-title":"J. Exp. Med."},{"key":"ref_33","doi-asserted-by":"crossref","unstructured":"Guerra, S., C\u00e1ceres, A., Knobeloch, K.P., Horak, I., and Esteban, M. (2008). Vaccinia virus E3 protein prevents the antiviral action of ISG15. PLoS. Pathog., 4.","DOI":"10.1371\/journal.ppat.1000096"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"34580","DOI":"10.1074\/jbc.M807029200","article-title":"Induction of protein kinase PKR-dependent activation of interferon regulatory factor 3 by vaccinia virus occurs through adapter IPS-1 signaling","volume":"283","author":"Zhang","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"6456180","DOI":"10.1155\/2017\/6456180","article-title":"Comparison of Host Gene Expression Profiles in Spleen Tissues of Genetically Susceptible and Resistant Mice during ECTV Infection","volume":"2017","author":"Cheng","year":"2017","journal-title":"Biomed. Res. Int."},{"key":"ref_36","doi-asserted-by":"crossref","unstructured":"Gregorczyk, K.P., Wy\u017cewski, Z., Szczepanowska, J., Toka, F.N., Mielcarska, M.B., Bossowska-Nowicka, M., Giery\u0144ska, M., Boraty\u0144ska-Jasi\u0144ska, A., Struzik, J., and Niemia\u0142towski, M.G. (2018). Ectromelia Virus Affects Mitochondrial Network Morphology, Distribution, and Physiology in Murine Fibroblasts and Macrophage Cell Line. Viruses, 10.","DOI":"10.3390\/v10050266"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"1749","DOI":"10.1016\/S0002-9440(10)64452-5","article-title":"Guanylate-binding protein-1 expression is selectively induced by inflammatory cytokines and is an activation marker of endothelial cells during inflammatory diseases","volume":"161","author":"Guenzi","year":"2002","journal-title":"Am. J. Pathol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"2140","DOI":"10.1073\/pnas.0711573105","article-title":"Kinetic analysis of a complete poxvirus transcriptome reveals an immediate-early class of genes","volume":"105","author":"Assarsson","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"26885","DOI":"10.1073\/pnas.2004688117","article-title":"Poxvirus-encoded TNF receptor homolog dampens inflammation and protects from uncontrolled lung pathology during respiratory infection","volume":"117","author":"Ng","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"e01407","DOI":"10.1128\/JVI.01407-20","article-title":"WGBP5 is an interferon-induced inhibitor of respiratory syncytial virus","volume":"94","author":"Li","year":"2020","journal-title":"J. Virol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1016\/j.chom.2016.02.019","article-title":"Guanylate binding protein (GBP) 5 is an interferon-inducible inhibitor of HIV-1 infectivity","volume":"19","author":"Krapp","year":"2016","journal-title":"Cell. Host. Microbe."},{"key":"ref_42","doi-asserted-by":"crossref","unstructured":"Zhu, Z., Shi, Z., Yan, W., Wei, J., Shao, J., Deng, X., Wang, S., Li, B., Tong, G., and Ma, Z. (2013). Nonstructural protein 1 of influenza A virus interacts with human guanylate-binding protein 1 to antagonize antiviral activity. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0055920"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1006\/viro.1999.9614","article-title":"Interferon-induced guanylate binding protein-1 (GBP-1) mediates an antiviral effect against vesicular stomatitis virus and encephalomyocarditis virus","volume":"256","author":"Anderson","year":"1999","journal-title":"Virology"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"2620","DOI":"10.1128\/AAC.00021-09","article-title":"Nonhuman primates are protected from smallpox virus or monkeypox virus challenges by the antiviral drug ST-246","volume":"53","author":"Huggins","year":"2009","journal-title":"Antimicrob. Agents. Chemother."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"2310","DOI":"10.1128\/JVI.00781-08","article-title":"Inhibition of a large double-stranded DNA virus by MxA protein","volume":"83","author":"Netherton","year":"2009","journal-title":"J. Virol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1186\/1743-422X-9-5","article-title":"In vitro inhibition of monkeypox virus production and spread by Interferon-beta","volume":"9","author":"Johnston","year":"2012","journal-title":"Virol. J."},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Lorenzo, M.M., Sanchez-Puig, J.M., and Blasco, R. (2017). Vaccinia virus and Cowpox virus are not susceptible to the interferon-induced antiviral protein MxA. PLoS ONE, 12.","DOI":"10.1371\/journal.pone.0181459"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"1290","DOI":"10.1096\/fj.11-189886","article-title":"A new splice variant of the human guanylate-binding protein 3 mediates anti-influenza activity through inhibition of viral transcription and replication","volume":"26","author":"Nordmann","year":"2012","journal-title":"FASEB J."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/j.jmb.2004.09.026","article-title":"Identification of residues in the human guanylate binding protein 1 critical for nucleotide binding and cooperative GTP hydrolysis","volume":"344","author":"Praefcke","year":"2004","journal-title":"J. Mol. Biol."},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Britzen-Laurent, N., Bauer, M., Berton, V., Fischer, N., Syguda, A., Reipschl\u00e4ger, S., Naschberger, E., Herrmann, C., and St\u00fcrzl, M. (2010). Intracellular trafficking of guanylate-binding proteins is regulated by heterodimerization in a hierarchical manner. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0014246"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"a010199","DOI":"10.1101\/cshperspect.a010199","article-title":"Poxvirus DNA replication","volume":"5","author":"Moss","year":"2013","journal-title":"Cold. Spring. Harb. Perspect. Biol."}],"container-title":["Microorganisms"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-2607\/11\/9\/2258\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T20:47:32Z","timestamp":1760129252000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-2607\/11\/9\/2258"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,9,8]]},"references-count":51,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2023,9]]}},"alternative-id":["microorganisms11092258"],"URL":"https:\/\/doi.org\/10.3390\/microorganisms11092258","relation":{},"ISSN":["2076-2607"],"issn-type":[{"value":"2076-2607","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,9,8]]}}}