{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T21:20:10Z","timestamp":1788470410996,"version":"build-2803163510"},"reference-count":57,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2023,3,1]],"date-time":"2023-03-01T00:00:00Z","timestamp":1677628800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Wellcome Trust","award":["105402\/Z\/14\/Z"],"award-info":[{"award-number":["105402\/Z\/14\/Z"]}]},{"name":"Wellcome Trust","award":["MR\/N013468\/1"],"award-info":[{"award-number":["MR\/N013468\/1"]}]},{"name":"Oxford Glycobiology endowment","award":["105402\/Z\/14\/Z"],"award-info":[{"award-number":["105402\/Z\/14\/Z"]}]},{"name":"Oxford Glycobiology endowment","award":["MR\/N013468\/1"],"award-info":[{"award-number":["MR\/N013468\/1"]}]},{"name":"Medical Research Council","award":["105402\/Z\/14\/Z"],"award-info":[{"award-number":["105402\/Z\/14\/Z"]}]},{"name":"Medical Research Council","award":["MR\/N013468\/1"],"award-info":[{"award-number":["MR\/N013468\/1"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Pathogens"],"abstract":"<jats:p>Crimean-Congo haemorrhagic fever virus (CCHFV) is a pathogen of increasing public health concern, being a widely distributed arbovirus and the causative agent of the potentially fatal Crimean-Congo haemorrhagic fever. Hazara virus (HAZV) is a genetically and serologically related virus that has been proposed as a surrogate for antiviral and vaccine testing for CCHFV. Glycosylation analysis of HAZV has been limited; first, we confirmed for the first time the occupation of two N-glycosylation sites in the HAZV glycoprotein. Despite this, there was no apparent antiviral efficacy of a panel of iminosugars against HAZV, as determined by quantification of the total secretion and infectious virus titres produced following infection of SW13 and Vero cells. This lack of efficacy was not due to an inability of deoxynojirimycin (DNJ)-derivative iminosugars to access and inhibit endoplasmic reticulum \u03b1-glucosidases, as demonstrated by free oligosaccharide analysis in uninfected and infected SW13 and uninfected Vero cells. Even so, iminosugars may yet have potential as antivirals for CCHFV since the positions and importance of N-linked glycans may differ between the viruses, a hypothesis requiring further evaluation.<\/jats:p>","DOI":"10.3390\/pathogens12030399","type":"journal-article","created":{"date-parts":[[2023,3,2]],"date-time":"2023-03-02T02:10:59Z","timestamp":1677723059000},"page":"399","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":7,"title":["Exploring the Potential of Iminosugars as Antivirals for Crimean-Congo Haemorrhagic Fever Virus, Using the Surrogate Hazara Virus: Liquid-Chromatography-Based Mapping of Viral N-Glycosylation and In Vitro Antiviral Assays"],"prefix":"10.3390","volume":"12","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-2912-6419","authenticated-orcid":false,"given":"Beatrice E.","family":"Tyrrell","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Kavli Institute for Nanoscience Discovery, University of Oxford, Oxford OX1 3QU, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3181-5291","authenticated-orcid":false,"given":"Abhinav","family":"Kumar","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Kavli Institute for Nanoscience Discovery, University of Oxford, Oxford OX1 3QU, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7466-2977","authenticated-orcid":false,"given":"Bevin","family":"Gangadharan","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Kavli Institute for Nanoscience Discovery, University of Oxford, Oxford OX1 3QU, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1330-9109","authenticated-orcid":false,"given":"Dominic","family":"Alonzi","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Kavli Institute for Nanoscience Discovery, University of Oxford, Oxford OX1 3QU, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0964-3681","authenticated-orcid":false,"given":"Juliane","family":"Brun","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Kavli Institute for Nanoscience Discovery, University of Oxford, Oxford OX1 3QU, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michelle","family":"Hill","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Kavli Institute for Nanoscience Discovery, University of Oxford, Oxford OX1 3QU, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6772-2855","authenticated-orcid":false,"given":"Tehmina","family":"Bharucha","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Kavli Institute for Nanoscience Discovery, University of Oxford, Oxford OX1 3QU, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0780-4362","authenticated-orcid":false,"given":"Andrew","family":"Bosworth","sequence":"additional","affiliation":[{"name":"UK Health Security Agency (UKHSA), Porton Down, Salisbury SP4 0JG, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Victoria","family":"Graham","sequence":"additional","affiliation":[{"name":"UK Health Security Agency (UKHSA), Porton Down, Salisbury SP4 0JG, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stuart","family":"Dowall","sequence":"additional","affiliation":[{"name":"UK Health Security Agency (UKHSA), Porton Down, Salisbury SP4 0JG, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4383-4641","authenticated-orcid":false,"given":"Joanna L.","family":"Miller","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Kavli Institute for Nanoscience Discovery, University of Oxford, Oxford OX1 3QU, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1969-4949","authenticated-orcid":false,"given":"Nicole","family":"Zitzmann","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Kavli Institute for Nanoscience Discovery, University of Oxford, Oxford OX1 3QU, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,3,1]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.antiviral.2015.05.005","article-title":"Meeting report: First International Conference on Crimean-Congo hemorrhagic fever","volume":"120","author":"Papa","year":"2015","journal-title":"Antivir. Res."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/j.jcv.2009.11.007","article-title":"The efficacy of ribavirin in the treatment of Crimean-Congo hemorrhagic fever in Eastern Black Sea region in Turkey","volume":"47","author":"Koksal","year":"2010","journal-title":"J. Clin. Virol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"3432","DOI":"10.1093\/jac\/dkz328","article-title":"Identification of the crucial parameters regarding the efficacy of ribavirin therapy in Crimean-Congo haemorrhagic fever (CCHF) patients: A systematic review and meta-analysis","volume":"74","author":"Jabbari","year":"2019","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_4","first-page":"Cd012713","article-title":"Ribavirin for treating Crimean Congo haemorrhagic fever","volume":"2018","author":"Johnson","year":"2018","journal-title":"Cochrane Database Syst. Rev."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1080\/1040841X.2016.1242868","article-title":"Iminosugars: Promising therapeutics for influenza infection","volume":"43","author":"Tyrrell","year":"2017","journal-title":"Crit. Rev. Microbiol."},{"key":"ref_6","doi-asserted-by":"crossref","unstructured":"Callahan, M., Treston, A.M., Lin, G., Smith, M., Kaufman, B., Khaliq, M., DeWald, L.E., Spurgers, K., Warfield, K.L., and Lowe, P. (2022). Randomized single oral dose phase 1 study of safety, tolerability, and pharmacokinetics of iminosugar UV-4 hydrochloride (UV-4B) in healthy subjects. PLoS Negl. Trop. Dis., 16.","DOI":"10.1371\/journal.pntd.0010636"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"104551","DOI":"10.1016\/j.antiviral.2019.104551","article-title":"Iminosugars counteract the downregulation of the interferon \u03b3 receptor by dengue virus","volume":"170","author":"Miller","year":"2019","journal-title":"Antivir. Res."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1007\/978-981-10-8727-1_20","article-title":"Mechanisms of antiviral activity of iminosugars against dengue virus","volume":"1062","author":"Miller","year":"2018","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"105269","DOI":"10.1016\/j.antiviral.2022.105269","article-title":"Antiviral effects of deoxynojirimycin (DNJ)-based iminosugars in dengue virus-infected primary dendritic cells","volume":"199","author":"Perera","year":"2022","journal-title":"Antivir. Res."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1111\/imm.13393","article-title":"Pathogen-induced inflammation is attenuated by the iminosugar MON-DNJ via modulation of the unfolded protein response","volume":"164","author":"Sayce","year":"2021","journal-title":"Immunology"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"4205","DOI":"10.1021\/acs.jmedchem.0c00067","article-title":"Targeting endoplasmic reticulum \u03b1-glucosidase I with a single-dose iminosugar treatment protects against lethal influenza and dengue virus infections","volume":"63","author":"Warfield","year":"2020","journal-title":"J. Med. Chem."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"7484","DOI":"10.1038\/s41598-019-43030-y","article-title":"Lack of selective resistance of influenza A virus in presence of host-targeted antiviral, UV-4B","volume":"9","author":"Warfield","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1016\/j.virol.2006.11.023","article-title":"N-linked glycosylation of Gn (but not Gc) is important for Crimean Congo hemorrhagic fever virus glycoprotein localization and transport","volume":"361","author":"Erickson","year":"2007","journal-title":"Virology"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"8834","DOI":"10.1128\/JVI.00752-06","article-title":"Crimean-Congo hemorrhagic fever virus genomics and global diversity","volume":"80","author":"Deyde","year":"2006","journal-title":"J. Virol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"6152","DOI":"10.1128\/JVI.79.10.6152-6161.2005","article-title":"Cellular localization and antigenic characterization of crimean-congo hemorrhagic fever virus glycoproteins","volume":"79","author":"Smith","year":"2005","journal-title":"J. Virol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1186\/1743-422X-8-249","article-title":"Inhibition of Hazara nairovirus replication by small interfering RNAs and their combination with ribavirin","volume":"8","author":"Flusin","year":"2011","journal-title":"Virol. J."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1099\/0022-1317-53-1-169","article-title":"Structural polypeptides of Hazara virus","volume":"53","author":"Foulke","year":"1981","journal-title":"J. Gen. Virol."},{"key":"ref_18","doi-asserted-by":"crossref","unstructured":"Kuhn, J.H., Wiley, M.R., Rodriguez, S.E., B\u00e0o, Y., Prieto, K., Travassos da Rosa, A.P., Guzman, H., Savji, N., Ladner, J.T., and Tesh, R.B. (2016). Genomic characterization of the genus nairovirus (family Bunyaviridae). Viruses, 8.","DOI":"10.3390\/v8060164"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"594","DOI":"10.3181\/00379727-146-38154","article-title":"Cross plaque neutralization tests with cloned Crimean hemorrhagic fever-Congo (CHF-C) and Hazara viruses","volume":"146","author":"Buckley","year":"1974","journal-title":"Proc. Soc. Exp. Biol. Med."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1159\/000149175","article-title":"The nairovirus genus: Serological relationships","volume":"14","author":"Casals","year":"1980","journal-title":"Intervirology"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"560","DOI":"10.1099\/vir.0.038455-0","article-title":"Hazara virus infection is lethal for adult type I interferon receptor-knockout mice and may act as a surrogate for infection with the human-pathogenic Crimean\u2013Congo hemorrhagic fever virus","volume":"93","author":"Dowall","year":"2012","journal-title":"J. Gen. Virol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1093\/oxfordjournals.aje.a121197","article-title":"Tick-borne viruses of West Pakistan. II. Hazara virus, a new agent isolated from Ixodes redikorzevi ticks from the Kaghan Valley, W. Pakistan","volume":"92","author":"Begum","year":"1970","journal-title":"Am. J. Epidemiol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1093\/oxfordjournals.aje.a121196","article-title":"Tick-borne viruses of West Pakistan. I. Isolation and general characteristics","volume":"92","author":"Begum","year":"1970","journal-title":"Am. J. Epidemiol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"7263","DOI":"10.1128\/JVI.76.14.7263-7275.2002","article-title":"Characterization of the glycoproteins of Crimean-Congo hemorrhagic fever virus","volume":"76","author":"Sanchez","year":"2002","journal-title":"J. Virol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"20213","DOI":"10.1038\/srep20213","article-title":"Tofla virus: A newly identified nairovirus of the Crimean-Congo hemorrhagic fever group isolated from ticks in Japan","volume":"6","author":"Shimada","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"514","DOI":"10.1128\/JVI.80.1.514-525.2006","article-title":"Crimean-Congo hemorrhagic fever virus glycoprotein precursor is cleaved by furin-like and SKI-1 proteases to generate a novel 38-kilodalton glycoprotein","volume":"80","author":"Sanchez","year":"2006","journal-title":"J. Virol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"9937","DOI":"10.1074\/jbc.RA118.002494","article-title":"Potassium is a trigger for conformational change in the fusion spike of an enveloped RNA virus","volume":"293","author":"Punch","year":"2018","journal-title":"J. Biol. Chem."},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"Chauhan, J.S., Rao, A., and Raghava, G.P.S. (2013). In silico platform for prediction of N-, O- and C-glycosites in eukaryotic protein sequences. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0067008"},{"key":"ref_29","unstructured":"Gupta, R., Jung, E., and Brunak, S. (2020, May 27). Prediction of N-Glycosylation Sites in Human Proteins. Available online: https:\/\/services.healthtech.dtu.dk\/service.php?NetNGlyc-1.0."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"9305","DOI":"10.1128\/JVI.00661-16","article-title":"Heat shock protein 70 family members interact with Crimean-Congo hemorrhagic fever virus and Hazara virus nucleocapsid proteins and perform a functional role in the nairovirus replication cycle","volume":"90","author":"Surtees","year":"2016","journal-title":"J. Virol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"586","DOI":"10.1021\/acscentsci.1c00058","article-title":"Assessing Antigen Structural Integrity through Glycosylation Analysis of the SARS-CoV-2 Viral Spike","volume":"7","author":"Brun","year":"2021","journal-title":"ACS Cent. Sci."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"12072","DOI":"10.1038\/s41598-017-12229-2","article-title":"Absolute quantitation of disease protein biomarkers in a single LC-MS acquisition using apolipoprotein F as an example","volume":"7","author":"Kumar","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/j.antiviral.2010.04.007","article-title":"A novel nucleoside analog, 1-beta-d-ribofuranosyl-3-ethynyl-[1,2,4]triazole (ETAR), exhibits efficacy against a broad range of flaviviruses in vitro","volume":"87","author":"McDowell","year":"2010","journal-title":"Antivir. Res."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1042\/BST20160182","article-title":"Iminosugar antivirals: The therapeutic sweet spot","volume":"45","author":"Alonzi","year":"2017","journal-title":"Biochem. Soc. Trans."},{"key":"ref_35","unstructured":"Gupta, R., and Brunak, S. (2002). Biocomputing 2002: Proceedings of the Pacific Symposium on Biocomputing Pacific Symposium on Biocomputing, Kauai, Hawaii, USA, 3\u20137 January 2002, World Scientific Publishing."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"8544","DOI":"10.1073\/pnas.1703682114","article-title":"Interdomain conformational flexibility underpins the activity of UGGT, the eukaryotic glycoprotein secretion checkpoint","volume":"114","author":"Roversi","year":"2017","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1093\/glycob\/4.2.141","article-title":"Introduction of oxygen into the alkyl chain of N-decyl-dNM decreases lipophilicity and results in increased retention of glucose residues on N-linked oligosaccharides","volume":"4","author":"Tan","year":"1994","journal-title":"Glycobiology"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1042\/BJ20031822","article-title":"Cellular effects of deoxynojirimycin analogues: Uptake, retention and inhibition of glycosphingolipid biosynthesis","volume":"381","year":"2004","journal-title":"Biochem. J."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1093\/trstmh\/trv050","article-title":"The global distribution of Crimean-Congo hemorrhagic fever","volume":"109","author":"Messina","year":"2015","journal-title":"Trans. R. Soc. Trop. Med. Hyg."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1215","DOI":"10.1093\/jac\/dkr136","article-title":"Ribavirin for patients with Crimean\u2013Congo haemorrhagic fever: A systematic review and meta-analysis","volume":"66","author":"Ascioglu","year":"2011","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"581","DOI":"10.4269\/ajtmh.1989.41.581","article-title":"Inhibition of Crimean-Congo hemorrhagic fever viral infectivity yields in vitro by ribavirin","volume":"41","author":"Watts","year":"1989","journal-title":"Am. J. Trop. Med. Hyg."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.antiviral.2003.11.006","article-title":"A simple assay for determining antiviral activity against Crimean-Congo hemorrhagic fever virus","volume":"62","author":"Paragas","year":"2004","journal-title":"Antivir. Res."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1016\/0166-3542(93)90040-P","article-title":"Ribavirin efficacy in an in vivo model of Crimean-Congo hemorrhagic fever virus (CCHF) infection","volume":"22","author":"Tignor","year":"1993","journal-title":"Antivir. Res."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"11089","DOI":"10.1128\/JVI.01383-10","article-title":"Pathogenesis and immune response of Crimean-Congo hemorrhagic fever virus in a STAT-1 knockout mouse model","volume":"84","author":"Bente","year":"2010","journal-title":"J. Virol."},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Oestereich, L., Rieger, T., Neumann, M., Bernreuther, C., Lehmann, M., Krasemann, S., Wurr, S., Emmerich, P., De Lamballerie, X., and \u00d6lschl\u00e4ger, S. (2014). Evaluation of antiviral efficacy of ribavirin, arbidol, and T-705 (favipiravir) in a mouse model for Crimean-Congo hemorrhagic fever. PLoS Negl. Trop. Dis., 8.","DOI":"10.1371\/journal.pntd.0002804"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/j.antiviral.2018.06.013","article-title":"Favipiravir (T-705) but not ribavirin is effective against two distinct strains of Crimean-Congo hemorrhagic fever virus in mice","volume":"157","author":"Hawman","year":"2018","journal-title":"Antivir. Res."},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Soares-Weiser, K., Thomas, S., Thomson, G., and Garner, P. (2010). Ribavirin for Crimean-Congo hemorrhagic fever: Systematic review and meta-analysis. BMC Infect. Dis., 10.","DOI":"10.1186\/1471-2334-10-207"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.antiviral.2016.03.001","article-title":"Inhibition of endoplasmic reticulum glucosidases is required for in vitro and in vivo dengue antiviral activity by the iminosugar UV-4","volume":"129","author":"Warfield","year":"2016","journal-title":"Antivir. Res."},{"key":"ref_49","doi-asserted-by":"crossref","unstructured":"Sayce, A.C., Alonzi, D.S., Killingbeck, S.S., Tyrrell, B.E., Hill, M.L., Caputo, A.T., Iwaki, R., Kinami, K., Ide, D., and Kiappes, J.L. (2016). Iminosugars inhibit dengue virus production via inhibition of ER alpha-glucosidases\u2014Not glycolipid processing enzymes. PLoS Negl. Trop. Dis., 10.","DOI":"10.1371\/journal.pntd.0004524"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"8698","DOI":"10.1128\/JVI.79.14.8698-8706.2005","article-title":"Castanospermine, a potent inhibitor of dengue virus infection in vitro and in vivo","volume":"79","author":"Whitby","year":"2005","journal-title":"J. Virol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/j.antiviral.2015.12.008","article-title":"Optimizing celgosivir therapy in mouse models of dengue virus infection of serotypes 1 and 2: The search for a window for potential therapeutic efficacy","volume":"127","author":"Watanabe","year":"2016","journal-title":"Antivir. Res."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1093\/glycob\/8.7.725","article-title":"Processing of viral envelope glycoprotein by the endomannosidase pathway: Evaluation of host cell specificity","volume":"8","author":"Karaivanova","year":"1998","journal-title":"Glycobiology"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1083\/jcb.117.3.551","article-title":"Opposite polarity of virus budding and of viral envelope glycoprotein distribution in epithelial cells derived from different tissues","volume":"117","author":"Zurzolo","year":"1992","journal-title":"J. Cell Biol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"2235","DOI":"10.1073\/pnas.91.6.2235","article-title":"Secretion of human hepatitis B virus is inhibited by the imino sugar N-butyldeoxynojirimycin","volume":"91","author":"Block","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"2117","DOI":"10.1083\/jcb.108.6.2117","article-title":"Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP)","volume":"108","author":"Hurtley","year":"1989","journal-title":"J. Cell Biol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"7597","DOI":"10.1016\/S0021-9258(17)42832-8","article-title":"The formation of vesicular stomatitis virus (San Juan strain) becomes temperature-sensitive when glucose residues are retained on the oligosaccharides of the glycoprotein","volume":"259","author":"Schlesinger","year":"1984","journal-title":"J. Biol. Chem."},{"key":"ref_57","doi-asserted-by":"crossref","unstructured":"Zivcec, M., Scholte, F.E.M., Spiropoulou, C.F., Spengler, J.R., and Bergeron, \u00c9. (2016). Molecular insights into Crimean-Congo hemorrhagic fever virus. Viruses, 8.","DOI":"10.3390\/v8040106"}],"container-title":["Pathogens"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-0817\/12\/3\/399\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T18:45:23Z","timestamp":1760121923000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-0817\/12\/3\/399"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,3,1]]},"references-count":57,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2023,3]]}},"alternative-id":["pathogens12030399"],"URL":"https:\/\/doi.org\/10.3390\/pathogens12030399","relation":{},"ISSN":["2076-0817"],"issn-type":[{"value":"2076-0817","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,3,1]]}}}