This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.
Adasme MF, Linnemann KL, Bolz SN, Kaiser F, Salentin S, Haupt VJ, Schroeder M. PLIP 2021: Expanding the scope of the protein-ligand interaction profiler to DNA and RNA. Nucleic Acids Res. 2021;49(W1):W530–W534. https://doi.org/10.1093/nar/gkab294AdasmeMFLinnemannKLBolzSNKaiserFSalentinSHauptVJSchroederM. PLIP 2021: Expanding the scope of the protein-ligand interaction profiler to DNA and RNA. . 2021;49(W1):W530–W534. https://doi.org/10.1093/nar/gkab294Search in Google Scholar
Anderson SL, Carton JM, Lou J, Xing L, Rubin BY. Interferon-induced guanylate binding protein-1 (GBP-1) mediates an antiviral effect against vesicular stomatitis virus and encephalomyocarditis virus. Virology. 1999;256(1):8–14. https://doi.org/10.1006/viro.1999.9614AndersonSLCartonJMLouJXingLRubinBY. Interferon-induced guanylate binding protein-1 (GBP-1) mediates an antiviral effect against vesicular stomatitis virus and encephalomyocarditis virus. . 1999;256(1):8–14. https://doi.org/10.1006/viro.1999.9614Search in Google Scholar
Blanchet M, Sureau C. Analysis of the cytosolic domains of the hepatitis B virus envelope proteins for their function in viral particle assembly and infectivity. J Virol. 2006;80(24):11935–11945. https://doi.org/10.1128/JVI.00621-06BlanchetMSureauC. Analysis of the cytosolic domains of the hepatitis B virus envelope proteins for their function in viral particle assembly and infectivity. . 2006;80(24):11935–11945. https://doi.org/10.1128/JVI.00621-06Search in Google Scholar
Block TM, Guo H, Guo JT. Molecular virology of hepatitis B virus for clinicians. Clin Liver Dis. 2007;11(4):685–706. https://doi.org/10.1016/j.cld.2007.08.002BlockTMGuoHGuoJT. Molecular virology of hepatitis B virus for clinicians. . 2007;11(4):685–706. https://doi.org/10.1016/j.cld.2007.08.002Search in Google Scholar
Bruss V, Ganem D. The role of envelope proteins in hepatitis B virus assembly. Proc Natl Acad Sci USA. 1991;88(3):1059–1063. https://doi.org/10.1073/pnas.88.3.1059BrussVGanemD. The role of envelope proteins in hepatitis B virus assembly. . 1991;88(3):1059–1063. https://doi.org/10.1073/pnas.88.3.1059Search in Google Scholar
Dickinson MS, Kutsch M, Sistemich L, Hernandez D, Piro AS, Needham D, Lesser CF, Herrmann C, Coers J. LPS-aggregating proteins GBP1 and GBP2 are each sufficient to enhance caspase-4 activation both in cellulo and in vitro. Proc Natl Acad Sci USA. 2023;120(15):e2216028120. https://doi.org/10.1073/pnas.2216028120DickinsonMSKutschMSistemichLHernandezDPiroASNeedhamDLesserCFHerrmannCCoersJ. LPS-aggregating proteins GBP1 and GBP2 are each sufficient to enhance caspase-4 activation both in cellulo and in vitro. . 2023;120(15):e2216028120. https://doi.org/10.1073/pnas.2216028120Search in Google Scholar
Du Y, Broering R, Li X, Zhang X, Liu J, Yang D, Lu M.In vivo mouse models for hepatitis B virus infection and their application. Front Immunol. 2021;12:766534. https://doi.org/10.3389/fimmu.2021.766534DuYBroeringRLiXZhangXLiuJYangDLuM. In vivo mouse models for hepatitis B virus infection and their application. . 2021;12:766534. https://doi.org/10.3389/fimmu.2021.766534Search in Google Scholar
Feng S, Enosi Tuipulotu D, Pandey A, Jing W, Shen C, Ngo C, Tessema MB, Li FJ, Fox D, Mathur A, et al. Pathogen-selective killing by guanylate-binding proteins as a molecular mechanism leading to inflammasome signaling. Nat Commun. 2022;13(1):4395. https://doi.org/10.1038/s41467-022-32127-0FengSEnosiTuipulotuDPandeyAJingWShenCNgoCTessemaMBLiFJFoxDMathurAet al.Pathogen-selective killing by guanylate-binding proteins as a molecular mechanism leading to inflammasome signaling. . 2022;13(1):4395. https://doi.org/10.1038/s41467-022-32127-0Search in Google Scholar
Fisch D, Bando H, Clough B, Hornung V, Yamamoto M, Shenoy AR, Frickel EM. Human GBP1 is a microbe-specific gatekeeper of macrophage apoptosis and pyroptosis. EMBO J. 2019;38(13):e100926. https://doi.org/10.15252/embj.2018100926FischDBandoHCloughBHornungVYamamotoMShenoyARFrickelEM. Human GBP1 is a microbe-specific gatekeeper of macrophage apoptosis and pyroptosis. . 2019;38(13):e100926. https://doi.org/10.15252/embj.2018100926Search in Google Scholar
Ge GH, Ye Y, Zhou XB, Chen L, He C, Wen DF, Tan YW. Hepatitis B surface antigen levels of cessation of nucleos(t)ide analogs associated with virological relapse in hepatitis B surface antigennegative chronic hepatitis B patients. World J Gastroenterol. 2015;21(28):8653–8659. https://doi.org/10.3748/wjg.v21.i28.8653GeGHYeYZhouXBChenLHeCWenDFTanYW. Hepatitis B surface antigen levels of cessation of nucleos(t)ide analogs associated with virological relapse in hepatitis B surface antigennegative chronic hepatitis B patients. . 2015;21(28):8653–8659. https://doi.org/10.3748/wjg.v21.i28.8653Search in Google Scholar
Glitscher M, Himmelsbach K, Woytinek K, Schollmeier A, Johne R, Praefcke GJK, Hildt E. Identification of the interferon-inducible GTPase GBP1 as major restriction factor for the Hepatitis E virus. J Virol. 2021;95(7):e01564–20. https://doi.org/10.1128/JVI.01564-20GlitscherMHimmelsbachKWoytinekKSchollmeierAJohneRPraefckeGJKHildtE. Identification of the interferon-inducible GTPase GBP1 as major restriction factor for the Hepatitis E virus. . 2021;95(7):e01564–20. https://doi.org/10.1128/JVI.01564-20Search in Google Scholar
Honkala AT, Tailor D, Malhotra SV. Guanylate-binding protein 1: An emerging target in inflammation and cancer. Front Immunol. 2020;10:3139. https://doi.org/10.3389/fimmu.2019.03139HonkalaATTailorDMalhotraSV. Guanylate-binding protein 1: An emerging target in inflammation and cancer. . 2020;10:3139. https://doi.org/10.3389/fimmu.2019.03139Search in Google Scholar
Huang D, Wu D, Wang P, Wang Y, Yuan W, Hu D, Hu J, Wang Y, Tao R, Xiao F, Zhang X, Wang X, Han M, Luo X, Yan W, Ning Q. End-of-treatment HBcrAg and HBsAb levels identify durable functional cure after Peg-IFN-based therapy in patients with CHB. J Hepatol. 2022;77(1):42–54. https://doi.org/10.1016/j.jhep.2022.01.021HuangDWuDWangPWangYYuanWHuDHuJWangYTaoRXiaoFZhangXWangXHanMLuoXYanWNingQ. End-of-treatment HBcrAg and HBsAb levels identify durable functional cure after Peg-IFN-based therapy in patients with CHB. . 2022;77(1):42–54. https://doi.org/10.1016/j.jhep.2022.01.021Search in Google Scholar
Islam M, Kumar K, Sevak JK, Jindal A, Vyas AK, Ramakrishna G, Kottilil S, Sharma MK, Sarin SK, Trehanpati N. Immune drivers of HBsAg loss in HBeAg-negative CHB patients after stopping nucleotide analog and administration of Peg-IFN. Hepatol Commun. 2023;7(5):e0098. https://doi.org/10.1097/HC9.0000000000000098IslamMKumarKSevakJKJindalAVyasAKRamakrishnaGKottililSSharmaMKSarinSKTrehanpatiN. Immune drivers of HBsAg loss in HBeAg-negative CHB patients after stopping nucleotide analog and administration of Peg-IFN. . 2023;7(5):e0098. https://doi.org/10.1097/HC9.0000000000000098Search in Google Scholar
Itsui Y, Sakamoto N, Kakinuma S, Nakagawa M, Sekine-Osajima Y, Tasaka-Fujita M, Nishimura-Sakurai Y, Suda G, Karakama Y, Mishima K, et al. Antiviral effects of the interferon-induced protein guanylate binding protein 1 and its interaction with the hepatitis C virus NS5B protein. Hepatology. 2009;50(6):1727–1737. https://doi.org/10.1002/hep.23195ItsuiYSakamotoNKakinumaSNakagawaMSekine-OsajimaYTasaka-FujitaMNishimura-SakuraiYSudaGKarakamaYMishimaKet al.Antiviral effects of the interferon-induced protein guanylate binding protein 1 and its interaction with the hepatitis C virus NS5B protein. . 2009;50(6):1727–1737. https://doi.org/10.1002/hep.23195Search in Google Scholar
Lebossé F, Testoni B, Fresquet J, Facchetti F, Galmozzi E, Fournier M, Hervieu V, Berthillon P, Berby F, Bordes I, et al. Intrahepatic innate immune response pathways are downregulated in untreated chronic hepatitis B. J Hepatol. 2017;66(5):897–909. https://doi.org/10.1016/j.jhep.2016.12.024Lebossé F, TestoniBFresquetJFacchettiFGalmozziEFournierMHervieuVBerthillonPBerbyFBordesIet al.Intrahepatic innate immune response pathways are downregulated in untreated chronic hepatitis B. . 2017;66(5):897–909. https://doi.org/10.1016/j.jhep.2016.12.024Search in Google Scholar
Li LF, Yu J, Li Y, Wang J, Li S, Zhang L, Xia SL, Yang Q, Wang X, Yu S, et al. Guanylate-binding protein 1, an interferon-induced GTPase, exerts an antiviral activity against classical swine fever virus depending on its GTPase activity. J Virol. 2016;90(9):4412–4426. https://doi.org/10.1128/JVI.02718-15LiLFYuJLiYWangJLiSZhangLXiaSLYangQWangXYuSet al.Guanylate-binding protein 1, an interferon-induced GTPase exerts an antiviral activity against classical swine fever virus depending on its GTPase activity. . 2016;90(9):4412–4426. https://doi.org/10.1128/JVI.02718-15Search in Google Scholar
Li P, Jiang W, Yu Q, Liu W, Zhou P, Li J, Xu J, Xu B, Wang F, Shao F. Ubiquitination and degradation of GBPs by a Shigella effector to suppress host defence. Nature. 2017;551(7680):378–383. https://doi.org/10.1038/nature24467LiPJiangWYuQLiuWZhouPLiJXuJXuBWangFShaoF. Ubiquitination and degradation of GBPs by a Shigella effector to suppress host defence. . 2017;551(7680):378–383. https://doi.org/10.1038/nature24467Search in Google Scholar
Lin N, Wang L, Guo Z, Guo S, Liu C, Lin J, Wu S, Xu S, Guo H, Fang F, et al. miR-548c-3p targets TRIM22 to attenuate the Peg-IFN-α therapeutic efficacy in HBeAg-positive patients with chronic hepatitis B. Antiviral Res. 2023;213:105584. https://doi.org/10.1016/j.antiviral.2023.105584LinNWangLGuoZGuoSLiuCLinJWuSXuSGuoHFangFet al.miR-548c-3p targets TRIM22 to attenuate the Peg-IFN-α therapeutic efficacy in HBeAg-positive patients with chronic hepatitis B. . 2023;213:105584. https://doi.org/10.1016/j.antiviral.2023.105584Search in Google Scholar
Liu J, Wang T, Zhang W, Cheng Y, He Q, Wang FS. Effect of combination treatment based on interferon and nucleos(t)ide analogues on functional cure of chronic hepatitis B: A systematic review and meta-analysis. Hepatol Int. 2020;14(6):958–972. https://doi.org/10.1007/s12072-020-10099-xLiuJWangTZhangWChengYHeQWangFS. Effect of combination treatment based on interferon and nucleos(t)ide analogues on functional cure of chronic hepatitis B: A systematic review and meta-analysis. . 2020;14(6):958–972. https://doi.org/10.1007/s12072-020-10099-xSearch in Google Scholar
Mariappan V, Adikari S, Shanmugam L, Easow JM, Balakrishna Pillai A. Differential expression of interferon inducible protein: Guanylate binding protein (GBP1 and GBP2) in severe dengue. Free Radic Biol Med. 2023;194:131–146. https://doi.org/10.1016/j.freeradbiomed.2022.11.037MariappanVAdikariSShanmugamLEasowJMBalakrishna PillaiA. Differential expression of interferon inducible protein: Guanylate binding protein (GBP1 and GBP2) in severe dengue. . 2023;194:131–146. https://doi.org/10.1016/j.freeradbiomed.2022.11.037Search in Google Scholar
Mirpuri J, Brazil JC, Berardinelli AJ, Nasr TR, Cooper K, Schnoor M, Lin PW, Parkos CA, Louis NA. Commensal Escherichia coli reduces epithelial apoptosis through IFN-αA-mediated induction of guanylate binding protein-1 in human and murine models of developing intestine. J Immunol. 2010;184(12):7186–7195. https://doi.org/10.4049/jimmunol.0903116MirpuriJBrazilJCBerardinelliAJNasrTRCooperKSchnoorMLinPWParkosCALouisNA. Commensal Escherichia coli reduces epithelial apoptosis through IFN-αA-mediated induction of guanylate binding protein-1 in human and murine models of developing intestine. . 2010;184(12):7186–7195. https://doi.org/10.4049/jimmunol.0903116Search in Google Scholar
Mohammadi N, Lindgren H, Golovliov I, Eneslätt K, Yamamoto M, Martin A, Henry T, Sjöstedt A. Guanylate-binding proteins are critical for effective control of Francisella tularensis strains in a mouse co-culture system of adaptive immunity. Front Cell Infect Microbiol. 2020;10:594063. https://doi.org/10.3389/fcimb.2020.594063MohammadiNLindgrenHGolovliovIEneslättKYamamotoMMartinAHenryTSjöstedtA. Guanylate-binding proteins are critical for effective control of Francisella tularensis strains in a mouse co-culture system of adaptive immunity. . 2020;10:594063. https://doi.org/10.3389/fcimb.2020.594063Search in Google Scholar
Mutz P, Metz P, Lempp FA, Bender S, Qu B, Schöneweis K, Seitz S, Tu T, Restuccia A, Frankish J, et al. HBV bypasses the innate immune response and does not protect HCV from antiviral activity of interferon. Gastroenterology. 2018;154(6):1791–1804.e22. https://doi.org/10.1053/j.gastro.2018.01.044MutzPMetzPLemppFABenderSQuBSchöneweisKSeitzSTuTRestucciaAFrankishJet al.HBV bypasses the innate immune response and does not protect HCV from antiviral activity of interferon. . 2018;154(6):1791–1804.e22. https://doi.org/10.1053/j.gastro.2018.01.044Search in Google Scholar
Nguyen MH, Wong G, Gane E, Kao JH, Dusheiko G. Hepatitis B virus: Advances in prevention, diagnosis, and therapy. Clin Microbiol Rev. 2020;33(2):e00046-19. https://doi.org/10.1128/CMR.00046-19NguyenMHWongGGaneEKaoJHDusheikoG. Hepatitis B virus: Advancesin prevention, diagnosis, and therapy. . 2020;33(2):e00046–19. https://doi.org/10.1128/CMR.00046-19Search in Google Scholar
Nordmann A, Wixler L, Boergeling Y, Wixler V, Ludwig S. A new splice variant of the human guanylate-binding protein 3 mediates anti-influenza activity through inhibition of viral transcription and replication. FASEB J. 2012;26(3):1290–1300. https://doi.org/10.1096/fj.11-189886NordmannAWixlerLBoergelingYWixlerVLudwigS. A new splice variant of the human guanylate-binding protein 3 mediates anti-influenza activity through inhibition of viral transcription and replication. . 2012;26(3):1290–1300. https://doi.org/10.1096/fj.11-189886Search in Google Scholar
Pan W, Zuo X, Feng T, Shi X, Dai J. Guanylate-binding protein 1 participates in cellular antiviral response to dengue virus. Virol J. 2012;9:292. https://doi.org/10.1186/1743-422X-9-292PanWZuoXFengTShiXDaiJ. Guanylate-binding protein 1 participates in cellular antiviral response to dengue virus. . 2012;9:292. https://doi.org/10.1186/1743-422X-9-292Search in Google Scholar
Piratvisuth T, Marcellin P, Popescu M, Kapprell HP, Rothe V, Lu ZM. Hepatitis B surface antigen: Association with sustained response to peginterferon alfa-2a in hepatitis B e antigen-positive patients. Hepatol Int. 2013;7(2):429–436. https://doi.org/10.1007/s12072-011-9280-0PiratvisuthTMarcellinPPopescuMKapprellHPRotheVLuZM. Hepatitis B surface antigen: Association with sustained response to peginterferon alfa-2a in hepatitis B e antigen-positive patients. . 2013;7(2):429–436. https://doi.org/10.1007/s12072-011-9280-0Search in Google Scholar
Prakash B, Praefcke GJ, Renault L, Wittinghofer A, Herrmann C. Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins. Nature. 2000;403(6769):567–571. https://doi.org/10.1038/35000617PrakashBPraefckeGJRenaultLWittinghoferAHerrmannC. Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins. . 2000;403(6769):567–571. https://doi.org/10.1038/35000617Search in Google Scholar
Raninga N, Nayeem SM, Gupta S, Mullick R, Pandita E, Das S, Deep S, Sau AK. Stimulation of GMP formation in hGBP1 is mediated by W79 and its effect on the antiviral activity. FEBS J. 2021;288(9):2970–2988. https://doi.org/10.1111/febs.15611RaningaNNayeemSMGuptaSMullickRPanditaEDasSDeepSSauAK. Stimulation of GMP formation in hGBP1 is mediated by W79 and its effect on the antiviral activity. . 2021;288(9):2970–2988. https://doi.org/10.1111/febs.15611Search in Google Scholar
Ren JH, Hu JL, Cheng ST, Yu HB, Wong VKW, Law BYK, Yang YF, Huang Y, Liu Y, Chen WX, et al. SIRT3 restricts hepatitis B virus transcription and replication through epigenetic regulation of covalently closed circular DNA involving suppressor of variegation 3–9 homolog 1 and SET domain containing 1A histone methyltransferases. Hepatology. 2018;68(4):1260–1276. https://doi.org/10.1002/hep.29912RenJHHuJLChengSTYuHBWongVKWLawBYKYangYFHuangYLiuYChenWXet al.SIRT3 restricts hepatitis B virus transcription and replication through epigenetic regulation of covalently closed circular DNA involving suppressor of variegation 3–9 homolog 1 and SET domain containing 1A histone methyltransferases. . 2018;68(4):1260–1276. https://doi.org/10.1002/hep.29912Search in Google Scholar
Salerno D, Chiodo L, Alfano V, Floriot O, Cottone G, Paturel A, Pallocca M, Plissonnier ML, Jeddari S, Belloni L, et al. Hepatitis B protein HBx binds the DLEU2 lncRNA to sustain cccDNA and host cancer-related gene transcription. Gut. 2020;69(11):2016–2024. https://doi.org/10.1136/gutjnl-2019-319637SalernoDChiodoLAlfanoVFloriotOCottoneGPaturelAPalloccaMPlissonnierMLJeddariSBelloniLet al.Hepatitis B protein HBx binds the DLEU2 lncRNA to sustain cccDNA and host cancer-related gene transcription. . 2020;69(11):2016–2024. https://doi.org/10.1136/gutjnl-2019-319637Search in Google Scholar
Santos JC, Boucher D, Schneider LK, Demarco B, Dilucca M, Shkarina K, Heilig R, Chen KW, Lim RYH, Broz P. Human GBP1 binds LPS to initiate assembly of a caspase-4 activating platform on cytosolic bacteria. Nat Commun. 2020;11(1):3276. https://doi.org/10.1038/s41467-020-16889-zSantosJCBoucherDSchneiderLKDemarcoBDiluccaMShkarinaKHeiligRChenKWLimRYHBrozP. Human GBP1 binds LPS to initiate assembly of a caspase-4 activating platform on cytosolic bacteria. . 2020;11(1):3276. https://doi.org/10.1038/s41467-020-16889-zSearch in Google Scholar
Schoggins JW, Wilson SJ, Panis M, Murphy MY, Jones CT, Bieniasz P, Rice CM. A diverse range of gene products are effectors of the type I interferon antiviral response. Nature. 2011;472(7344):481–485. https://doi.org/10.1038/nature09907SchogginsJWWilsonSJPanisMMurphyMYJonesCTBieniaszPRiceCM. A diverse range of gene products are effectors of the type I interferon antiviral response. . 2011;472(7344):481–485. https://doi.org/10.1038/nature09907Search in Google Scholar
Sen GC, Peters GA. Viral stress-inducible genes. Adv Virus Res. 2007;70:233–263. https://doi.org/10.1016/S0065-3527(07)70006-4SenGCPetersGA. Viral stress-inducible genes. . 2007;70:233–263. https://doi.org/10.1016/S0065-3527(07)70006-4Search in Google Scholar
Shih C, Yang CC, Choijilsuren G, Chang CH, Liou AT. Hepatitis B virus. Trends Microbiol. 2018;26(4):386–387. https://doi.org/10.1016/j.tim.2018.01.009ShihCYangCCChoijilsurenGChangCHLiouAT. Hepatitis B virus. . 2018;26(4):386–387. https://doi.org/10.1016/j.tim.2018.01.009Search in Google Scholar
Suslov A, Boldanova T, Wang X, Wieland S, Heim MH. Hepatitis B virus does not interfere with innate immune responses in the human liver. Gastroenterology. 2018;154(6):1778–1790. https://doi.org/10.1053/j.gastro.2018.01.034SuslovABoldanovaTWangXWielandSHeimMH. Hepatitis B virus does not interfere with innate immune responses in the human liver. . 2018;154(6):1778–1790. https://doi.org/10.1053/j.gastro.2018.01.034Search in Google Scholar
Tessema MB, Tuipulotu DE, Oates CV, Brooks AG, Man SM, Londrigan SL, Reading PC. Mouse guanylate-binding protein 1 does not mediate antiviral activity against influenza virus in vitro or in vivo. Immunol Cell Biol. 2023;101(5):383–396. https://doi.org/10.1111/imcb.12627TessemaMBTuipulotuDEOatesCVBrooksAGManSMLondriganSLReadingPC. Mouse guanylate-binding protein 1 does not mediate antiviral activity against influenza virus in vitro or in vivo. . 2023;101(5):383–396. https://doi.org/10.1111/imcb.12627Search in Google Scholar
Thompson AJ, Nguyen T, Iser D, Ayres A, Jackson K, Littlejohn M, Slavin J, Bowden S, Gane EJ, Abbott W, et al. Serum hepatitis B surface antigen and hepatitis B e antigen titers: Disease phase influences correlation with viral load and intrahepatic hepatitis B virus markers. Hepatology. 2010;51(6):1933–44. https://doi.org/10.1002/hep.23571ThompsonAJNguyenTIserDAyresAJacksonKLittlejohnMSlavinJBowdenSGaneEJAbbottWet al.Serum hepatitis B surface antigen and hepatitis B e antigen titers: Disease phase influences correlation with viral load and intrahepatic hepatitis B virus markers. . 2010;51(6):1933–44. https://doi.org/10.1002/hep.23571Search in Google Scholar
Tretina K, Park ES, Maminska A, MacMicking JD. Interferon-induced guanylate-binding proteins: Guardians of host defense in health and disease. J Exp Med. 2019;216(3):482–500. https://doi.org/10.1084/jem.20182031TretinaKParkESMaminskaAMacMickingJD. Interferon-induced guanylate-binding proteins: Guardians of host defense in health and disease. . 2019;216(3):482–500. https://doi.org/10.1084/jem.20182031Search in Google Scholar
Tseng TN, Hu TH, Wang JH, Kuo YH, Hung CH, Lu SN, Jeng WJ, Chen CH. Incidence and factors associated with HBV relapse after cessation of entecavir or tenofovir in patients with HBsAg below 100 IU/ml. Clin Gastroenterol Hepatol. 2020;18(12):2803–2812.e2. https://doi.org/10.1016/j.cgh.2020.04.037TsengTNHuTHWangJHKuoYHHungCHLuSNJengWJChenCH. Incidence and factors associated with HBV relapse after cessation of entecavir or tenofovir in patients with HBsAg below 100 IU/ml. . 2020;18(12):2803–2812.e2. https://doi.org/10.1016/j.cgh.2020.04.037Search in Google Scholar
Tseng TN, Kuo YH, Hu TH, Hung CH, Wang JH, Lu SN, Chen CH. Kinetics in HBsAg after stopping entecavir or tenofovir in patients with virological relapse but not clinical relapse. Viruses. 2022;14(6):1189. https://doi.org/10.3390/v14061189TsengTNKuoYHHuTHHungCHWangJHLuSNChenCH. Kinetics in HBsAg after stopping entecavir or tenofovir in patients with virological relapse but not clinical relapse. . 2022;14(6):1189. https://doi.org/10.3390/v14061189Search in Google Scholar
UniProt Consortium. UniProt: The Universal Protein Knowledgebase in 2023. Nucleic Acids Res. 2023;51(D1):D523–D531. https://doi.org/10.1093/nar/gkac1052UniProtConsortium. UniProt: The Universal Protein Knowledgebase in 2023. . 2023;51(D1):D523–D531. https://doi.org/10.1093/nar/gkac1052Search in Google Scholar
Viganò M, Grossi G, Loglio A, Lampertico P. Treatment of hepatitis B: Is there still a role for interferon? Liver Int. 2018;38(Suppl_1):79–83. https://doi.org/10.1111/liv. 13635Viganò M, GrossiGLoglioALamperticoP. Treatment of hepatitis B: Is there still a role for interferon?. 2018;38(Suppl_1):79–83. https://doi.org/10.1111/liv. 13635Search in Google Scholar
Wong GLH, Gane E, Lok ASF. How to achieve functional cure of HBV: Stopping NUCs, adding interferon or new drug development? J Hepatol. 2022;76(6):1249–1262. https://doi.org/10.1016/j.jhep.2021.11.024WongGLHGaneELokASF. How to achieve functional cure of HBV: Stopping NUCs, adding interferon or new drug development?. 2022;76(6):1249–1262. https://doi.org/10.1016/j.jhep.2021.11.024Search in Google Scholar
Wu D, Wang P, Han M, Chen Y, Chen X, Xia Q, Yan W, Wan X, Zhu C, Xie Q, et al. Sequential combination therapy with interferon, interleukin-2 and therapeutic vaccine in entecavir-suppressed chronic hepatitis B patients: The Endeavor study. Hepatol Int. 2019;13(5):573–586. https://doi.org/10.1007/s12072-019-09956-1WuDWangPHanMChenYChenXXiaQYanWWanXZhuCXieQet al.Sequential combination therapy with interferon, interleukin-2 and therapeutic vaccine in entecavir-suppressed chronic hepatitis B patients: The Endeavor study. . 2019;13(5):573–586. https://doi.org/10.1007/s12072-019-09956-1Search in Google Scholar
Xu S, Huang J, Xun Z, Li S, Fu Y, Lin N, Wu W, Chen T, Liu C, Ou Q. IFIT3 is increased in serum from patients with chronic hepatitis B virus (HBV) infection and promotes the anti-HBV effect of interferon alpha via JAK-STAT2 in vitro. Microbiol Spectr. 2022;10(6):e0155722. https://doi.org/10.1128/spectrum.01557-22XuSHuangJXunZLiSFuYLinNWuWChenTLiuCOuQ. IFIT3 is increased in serum from patients with chronic hepatitis B virus (HBV) infection and promotes the anti-HBV effect of interferon alpha via JAK-STAT2 in vitro. . 2022;10(6):e0155722. https://doi.org/10.1128/spectrum.01557-22Search in Google Scholar
Yuen MF, Chen DS, Dusheiko GM, Janssen HLA, Lau DTY, Locarnini SA, Peters MG, Lai CL. Hepatitis B virus infection. Nat Rev Dis Primers. 2018;4:18035. https://doi.org/10.1038/nrdp.2018.35YuenMFChenDSDusheikoGMJanssenHLALauDTYLocarniniSAPetersMGLaiCL. Hepatitis B virus infection. . 2018;4:18035. https://doi.org/10.1038/nrdp.2018.35Search in Google Scholar
Yuen MF, Heo J, Jang JW, Yoon JH, Kweon YO, Park SJ, Tami Y, You S, Yates P, Tao Y, et al. Safety, tolerability and antiviral activity of the antisense oligonucleotide bepirovirsen in patients with chronic hepatitis B: A phase 2 randomized controlled trial. Nat Med. 2021;27(10):1725–1734. https://doi.org/10.1038/s41591-021-01513-4YuenMFHeoJJangJWYoonJHKweonYOParkSJTamiYYouSYatesPTaoYet al.Safety, tolerability and antiviral activity of the antisense oligonucleotide bepirovirsen in patients with chronic hepatitis B: A phase 2 randomized controlled trial. . 2021;27(10):1725–1734. https://doi.org/10.1038/s41591-021-01513-4Search in Google Scholar
Yuen MF, Lim SG, Plesniak R, Tsuji K, Janssen HLA, Pojoga C, Gadano A, Popescu CP, Stepanova T, Asselah T, et al.; B-Clear Study Group. Efficacy and safety of bepirovirsen in chronic hepatitis B infection. N Engl J Med. 2022;387(21):1957–1968. https://doi.org/10.1056/NEJMoa2210027YuenMFLimSGPlesniakRTsujiKJanssenHLAPojogaCGadanoAPopescuCPStepanovaTAsselahTet al.; B-Clear Study Group. . 2022;387(21):1957–1968. https://doi.org/10.1056/NEJMoa2210027Search in Google Scholar
Zhang R, Li Z, Tang YD, Su C, Zheng C. When human guanylate-binding proteins meet viral infections. J Biomed Sci. 2021;28(1):17. https://doi.org/10.1186/s12929-021-00716-8ZhangRLiZTangYDSuCZhengC. When human guanylate-binding proteins meet viral infections. . 2021;28(1):17. https://doi.org/10.1186/s12929-021-00716-8Search in Google Scholar