{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,22]],"date-time":"2026-04-22T01:49:51Z","timestamp":1776822591125,"version":"3.51.2"},"reference-count":37,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2023,9,1]],"date-time":"2023-09-01T00:00:00Z","timestamp":1693526400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,9,1]],"date-time":"2023-09-01T00:00:00Z","timestamp":1693526400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,9,1]],"date-time":"2023-09-01T00:00:00Z","timestamp":1693526400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2023,9,1]],"date-time":"2023-09-01T00:00:00Z","timestamp":1693526400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2023,9,1]],"date-time":"2023-09-01T00:00:00Z","timestamp":1693526400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2023,9,1]],"date-time":"2023-09-01T00:00:00Z","timestamp":1693526400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2023,9,1]],"date-time":"2023-09-01T00:00:00Z","timestamp":1693526400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Veterinary Microbiology"],"published-print":{"date-parts":[[2023,9]]},"DOI":"10.1016\/j.vetmic.2023.109843","type":"journal-article","created":{"date-parts":[[2023,8,1]],"date-time":"2023-08-01T08:53:39Z","timestamp":1690880019000},"page":"109843","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":4,"special_numbering":"C","title":["The GTPase activity and isoprenylation of Swine GBP1 are critical for inhibiting the production of Japanese Encephalitis Virus"],"prefix":"10.1016","volume":"284","author":[{"given":"Zhancheng","family":"Tian","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hongge","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ruiming","family":"Yu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Junzheng","family":"Du","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shandian","family":"Gao","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Qiongjie","family":"Wang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Guiquan","family":"Guan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hong","family":"Yin","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.vetmic.2023.109843_bib1","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":"10.1016\/j.vetmic.2023.109843_bib2","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1016\/j.antiviral.2018.06.014","article-title":"Genistein inhibits African swine fever virus replication in vitro by disrupting viral DNA synthesis","volume":"156","author":"Arabyan","year":"2018","journal-title":"Antivir. Res"},{"key":"10.1016\/j.vetmic.2023.109843_bib3","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":"10.1016\/j.vetmic.2023.109843_bib4","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0014246","article-title":"Intracellular trafficking of guanylate-binding proteins is regulated by heterodimerization in a hierarchical manner","volume":"5","author":"Britzen-Laurent","year":"2010","journal-title":"PLoS One"},{"key":"10.1016\/j.vetmic.2023.109843_bib5","first-page":"4717","article-title":"Interferon-induced guanylate-binding proteins lack an N(T)KXD consensus motif and bind GMP in addition to GDP and GTP","volume":"11","author":"Cheng","year":"1991","journal-title":"Mol. Cell Biol."},{"key":"10.1016\/j.vetmic.2023.109843_bib6","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":"10.1016\/j.vetmic.2023.109843_bib7","doi-asserted-by":"crossref","unstructured":"Glitscher, M., Himmelsbach, K.,\u00a0Woytinek, K.,\u00a0Schollmeier, A.,\u00a0Johne, R.,\u00a0Praefcke, G.J.K.,\u00a0Hildt, E.\u00a02021. Identification of the interferon-inducible GTPase GBP1 as major restriction factor for the Hepatitis E virus. J Virol.","DOI":"10.1128\/JVI.01564-20"},{"key":"10.1016\/j.vetmic.2023.109843_bib8","doi-asserted-by":"crossref","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":"10.1016\/j.vetmic.2023.109843_bib9","first-page":"11","article-title":"Decanoyl-Arg-Val-Lys-Arg-Chloromethylketone: an antiviral compound that acts against flaviviruses through the inhibition of furin-mediated prM Cleavage","author":"Imran","year":"2019","journal-title":"Virus -Basel"},{"key":"10.1016\/j.vetmic.2023.109843_bib10","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":"10.1016\/j.vetmic.2023.109843_bib11","first-page":"19","article-title":"The multifaceted roles of autophagy in flavivirus-host interactions","author":"Ke","year":"2018","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.vetmic.2023.109843_bib12","doi-asserted-by":"crossref","first-page":"7846","DOI":"10.1128\/JVI.00789-08","article-title":"A single N-linked glycosylation site in the Japanese encephalitis virus prM protein is critical for cell type-specific prM protein biogenesis, virus particle release, and pathogenicity in mice","volume":"82","author":"Kim","year":"2008","journal-title":"J. Virol."},{"key":"10.1016\/j.vetmic.2023.109843_bib13","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":"10.1016\/j.vetmic.2023.109843_bib14","doi-asserted-by":"crossref","DOI":"10.1016\/j.micpath.2020.104492","article-title":"The pre membrane and envelope protein is the crucial virulence determinant of Japanese encephalitis virus","volume":"148","author":"Leng","year":"2020","journal-title":"Microb. Pathog."},{"key":"10.1016\/j.vetmic.2023.109843_bib15","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":"10.1016\/j.vetmic.2023.109843_bib16","doi-asserted-by":"crossref","first-page":"2797","DOI":"10.1016\/j.molimm.2008.02.007","article-title":"Molecular characterization of the porcine GBP1 and GBP2 genes","volume":"45","author":"Ma","year":"2008","journal-title":"Mol. Immunol."},{"key":"10.1016\/j.vetmic.2023.109843_bib17","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1016\/j.it.2004.08.010","article-title":"IFN-inducible GTPases and immunity to intracellular pathogens","volume":"25","author":"MacMicking","year":"2004","journal-title":"Trends Immunol."},{"key":"10.1016\/j.vetmic.2023.109843_bib18","first-page":"810","article-title":"Progress in studies on the overwintering of the mosquito Culex tritaeniorhynchus","volume":"27","author":"Min","year":"1996","journal-title":"Southeast Asian J. Trop. Med Public Health"},{"key":"10.1016\/j.vetmic.2023.109843_bib19","doi-asserted-by":"crossref","first-page":"8680","DOI":"10.1073\/pnas.0503227102","article-title":"Golgi targeting of human guanylate-binding protein-1 requires nucleotide binding, isoprenylation, and an IFN-gamma-inducible cofactor","volume":"102","author":"Modiano","year":"2005","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.vetmic.2023.109843_bib20","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1002\/jlb.60.3.423","article-title":"Prenylation of an interferon-gamma-induced GTP-binding protein: the human guanylate binding protein, huGBP1","volume":"60","author":"Nantais","year":"1996","journal-title":"J. Leukoc. Biol."},{"key":"10.1016\/j.vetmic.2023.109843_bib21","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1089\/jir.2006.26.328","article-title":"In silico genomic analysis of the human and murine guanylate-binding protein (GBP) gene clusters","volume":"26","author":"Olszewski","year":"2006","journal-title":"J. Interferon Cytokine Res."},{"key":"10.1016\/j.vetmic.2023.109843_bib22","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1186\/1743-422X-9-292","article-title":"Guanylate-binding protein 1 participates in cellular antiviral response to dengue virus","volume":"9","author":"Pan","year":"2012","journal-title":"Virol. J."},{"key":"10.1016\/j.vetmic.2023.109843_bib23","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1006\/jmbi.1999.3062","article-title":"Nucleotide-binding characteristics of human guanylate-binding protein 1 (hGBP1) and identification of the third GTP-binding motif","volume":"292","author":"Praefcke","year":"1999","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.vetmic.2023.109843_bib24","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":"10.1016\/j.vetmic.2023.109843_bib25","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1016\/j.ijmm.2017.10.013","article-title":"Regulation of innate immune functions by guanylate-binding proteins","volume":"308","author":"Praefcke","year":"2018","journal-title":"Int. J. Med. Microbiol"},{"key":"10.1016\/j.vetmic.2023.109843_bib26","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1038\/35000617","article-title":"Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins","volume":"403","author":"Prakash","year":"2000","journal-title":"Nature"},{"key":"10.1016\/j.vetmic.2023.109843_bib27","doi-asserted-by":"crossref","first-page":"11800","DOI":"10.1128\/JVI.05237-11","article-title":"A fusion-loop antibody enhances the infectious properties of immature flavivirus particles","volume":"85","author":"Rodenhuis-Zybert","year":"2011","journal-title":"J. Virol."},{"key":"10.1016\/j.vetmic.2023.109843_bib28","doi-asserted-by":"crossref","first-page":"1965","DOI":"10.1099\/vir.0.044453-0","article-title":"Identification of residues in West Nile virus pre-membrane protein that influence viral particle secretion and virulence","volume":"93","author":"Setoh","year":"2012","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.vetmic.2023.109843_bib29","first-page":"171","article-title":"Pathogenesis and clinical features of Japanese encephalitis and West Nile virus infections","volume":"267","author":"Solomon","year":"2002","journal-title":"Curr. Top. Microbiol Immunol."},{"key":"10.1016\/j.vetmic.2023.109843_bib30","doi-asserted-by":"crossref","first-page":"2191","DOI":"10.1091\/mbc.11.7.2191","article-title":"Murine guanylate-binding protein: incomplete geranylgeranyl isoprenoid modification of an interferon-gamma-inducible guanosine triphosphate-binding protein","volume":"11","author":"Stickney","year":"2000","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.vetmic.2023.109843_bib31","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1084\/jem.20182031","article-title":"Interferon-induced guanylate-binding proteins: guardians of host defense in health and disease","volume":"216","author":"Tretina","year":"2019","journal-title":"J. Exp. Med"},{"key":"10.1016\/j.vetmic.2023.109843_bib32","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1111\/j.1742-4658.2011.08415.x","article-title":"The guanine cap of human guanylate-binding protein 1 is responsible for dimerization and self-activation of GTP hydrolysis","volume":"279","author":"Wehner","year":"2012","journal-title":"FEBS J."},{"key":"10.1016\/j.vetmic.2023.109843_bib33","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1099\/vir.0.035964-0","article-title":"A conserved region in the prM protein is a critical determinant in the assembly of flavivirus particles","volume":"93","author":"Yoshii","year":"2012","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.vetmic.2023.109843_bib34","first-page":"1314","article-title":"Comparson of the immunogenicity of genotypeJapanese encephalitis virus subunit vaccine candidate antigens","volume":"36","author":"Yu","year":"2020","journal-title":"Sheng Wu Gong. Cheng Xue Bao"},{"key":"10.1016\/j.vetmic.2023.109843_bib35","doi-asserted-by":"crossref","first-page":"933","DOI":"10.1126\/science.aam7120","article-title":"A single mutation in the prM protein of Zika virus contributes to fetal microcephaly","volume":"358","author":"Yuan","year":"2017","journal-title":"Science"},{"key":"10.1016\/j.vetmic.2023.109843_bib36","article-title":"Nonstructural protein 1 of influenza A virus interacts with human guanylate-binding protein 1 to antagonize antiviral activity","volume":"8","author":"Zhu","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.vetmic.2023.109843_bib37","first-page":"91","article-title":"Guanylate-Binding Protein 1 Inhibits Nuclear Delivery of Kaposi's Sarcoma-associated herpesvirus virions by disrupting formation of actin filament","author":"Zou","year":"2017","journal-title":"J. Virol."}],"container-title":["Veterinary Microbiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0378113523001955?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0378113523001955?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,7]],"date-time":"2025-10-07T23:24:51Z","timestamp":1759879491000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0378113523001955"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,9]]},"references-count":37,"alternative-id":["S0378113523001955"],"URL":"https:\/\/doi.org\/10.1016\/j.vetmic.2023.109843","relation":{},"ISSN":["0378-1135"],"issn-type":[{"value":"0378-1135","type":"print"}],"subject":[],"published":{"date-parts":[[2023,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The GTPase activity and isoprenylation of Swine GBP1 are critical for inhibiting the production of Japanese Encephalitis Virus","name":"articletitle","label":"Article Title"},{"value":"Veterinary Microbiology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.vetmic.2023.109843","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2023 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"109843"}}