{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,3]],"date-time":"2026-04-03T15:15:27Z","timestamp":1775229327872,"version":"3.50.1"},"reference-count":56,"publisher":"Central Research Institute for Epidemiology","issue":"1","license":[{"start":{"date-parts":[[2026,2,28]],"date-time":"2026-02-28T00:00:00Z","timestamp":1772236800000},"content-version":"unspecified","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"content-domain":{"domain":["virusjour.crie.ru"],"crossmark-restriction":false},"short-container-title":["Problems of Virology"],"abstract":"<jats:p>Investigating the mechanisms of viral attachment and entry into cells is crucial for understanding viral pathogenesis and developing therapeutic strategies. The aim of this review is to characterize pseudo-typed particles based on the vesicular stomatitis virus (VSV) as a convenient and effective tool for studying viral entry into cells, based on literature data (PubMed, Scopus, and Web of Science), and to determine the prospects for combining this method with genetic and protein-based approaches.\r\nVSV, a member of the Rhabdoviridae family, has a remarkable capacity for pseudotyping, which involves the replacement of its native glycoprotein (G) with envelope proteins from other viruses. This feature enables the modeling of the cell entry process without the need for wild-type viruses. The VSV genome is modified by deleting the G gene and incorporating reporter genes (e.g., GFP or luciferase), thereby facilitating the quantitative assessment of infectivity.\r\nThe methodology for generating pseudoviruses involves a two-plasmid cotransfection system in cell lines (e.g., HEK293T), with plasmids encoding the VSV structural proteins and the target viral envelope proteins. The advantages of the VSV system include high particle titers, rapid reporter signal manifestation, and the feasibility of work under Biosafety Level 2 conditions. However, limitations are associated with differences in the distribution of viral proteins on the surface of pseudoviruses compared to native virions, necessitating additional data validation. Conclusion. Methods for analyzing virus-cell interactions were studied, such as Virus Overlay Protein Binding Assay (VOPBA), RNA interference, CRISPR\/Cas9 knockout, and gene overexpression. These approaches allow for the identification of cellular receptors, investigation of specific protein functions, and assessment of the impact of mutations. Future prospects for the application of VSV pseudoviruses include screening viral entry inhibitors, analyzing antibody neutralization, and vaccine development. Despite technical limitations, pseudotyped particles remain an indispensable tool for studying highly pathogenic and fastidious viruses. For the present review, a literature search was conducted in the PubMed, Scopus, and Web of Science databases.<\/jats:p>","DOI":"10.36233\/0507-4088-360","type":"journal-article","created":{"date-parts":[[2026,3,23]],"date-time":"2026-03-23T17:24:39Z","timestamp":1774286679000},"page":"13-20","update-policy":"https:\/\/doi.org\/10.36233\/0372-9311-crossmark","source":"Crossref","is-referenced-by-count":0,"title":["The application of pseudotyped viruses based on vesicular stomatitis virus (&lt;i&gt;Rhabdoviridae, Vesiculovirus&lt;\/i&gt;) in order to study the interaction of viruses with cells"],"prefix":"10.36233","volume":"71","author":[{"ORCID":"https:\/\/orcid.org\/0009-0005-1988-2853","authenticated-orcid":false,"given":"Nikita O.","family":"Akimov","sequence":"additional","affiliation":[{"name":"Saint-Petersburg Pasteur Institute"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8730-4872","authenticated-orcid":false,"given":"Anna S.","family":"Dolgova","sequence":"additional","affiliation":[{"name":"Saint-Petersburg Pasteur Institute"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"22004","published-online":{"date-parts":[[2026,2,28]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","unstructured":"Whitt M.A. Generation of VSV pseudotypes using recombinant \u0394G-VSV for studies on virus entry, identification of entry inhibitors, and immune responses to vaccines. J. Virol. Methods. 2010; 169(2): 365\u201374. https:\/\/doi.org\/10.1016\/j.jviromet.2010.08.006","DOI":"10.1016\/j.jviromet.2010.08.006"},{"key":"ref2","doi-asserted-by":"crossref","unstructured":"Fukushi S., Watanabe R., Taguchi F. Pseudotyped vesicular stomatitis virus for analysis of virus entry mediated by SARS coronavirus spike proteins. Methods Mol. Biol. 2008; 454: 331\u20138. https:\/\/doi.org\/10.1007\/978-1-59745-181-9_23","DOI":"10.1007\/978-1-59745-181-9_23"},{"key":"ref3","doi-asserted-by":"crossref","unstructured":"Walker P.J., Firth C., Widen S.G., Blasdell K.R., Guzman H., Wood T.G., et al. Evolution of genome size and complexity in the rhabdoviridae. PLoS Pathog. 2015; 11(2): e1004664. https:\/\/doi.org\/10.1371\/journal.ppat.1004664","DOI":"10.1371\/journal.ppat.1004664"},{"key":"ref4","doi-asserted-by":"crossref","unstructured":"Rodriguez L.L., Pauszek S.J., Bunch T.A., Schumann K.R. Full-length genome analysis of natural isolates of vesicular stomatitis virus (Indiana 1 serotype) from North, Central and South America. J. Gen. Virol. 2002; 83(Pt. 10): 2475\u201383. https:\/\/doi.org\/10.1099\/0022-1317-83-10-2475","DOI":"10.1099\/0022-1317-83-10-2475"},{"key":"ref5","doi-asserted-by":"crossref","unstructured":"Ge P., Tsao J., Schein S., Green T.J., Luo M., Zhou Z.H. Cryo-EM model of the bullet-shaped vesicular stomatitis virus. Science. 2010; 327(5966): 689\u201393. https:\/\/doi.org\/10.1126\/science.1181766","DOI":"10.1126\/science.1181766"},{"key":"ref6","doi-asserted-by":"crossref","unstructured":"Green T.J., Zhang X., Wertz G.W., Luo M. Structure of the vesicular stomatitis virus nucleoprotein-RNA complex. Science. 2006; 313(5785): 357\u201360. https:\/\/doi.org\/10.1126\/science.1126953","DOI":"10.1126\/science.1126953"},{"key":"ref7","doi-asserted-by":"crossref","unstructured":"Iseni F., Baudin F., Blondel D., Ruigrok R.W. Structure of the RNA inside the vesicular stomatitis virus nucleocapsid. RNA. 2000; 6(2): 270\u201381. https:\/\/doi.org\/10.1017\/S135583820099109X","DOI":"10.1017\/S135583820099109X"},{"key":"ref8","doi-asserted-by":"crossref","unstructured":"Ogino T., Green T.J. RNA synthesis and capping by non-segmented negative strand RNA viral polymerases: lessons from a prototypic virus. Front. Microbiol. 2019; 10: 1490. https:\/\/doi.org\/10.3389\/fmicb.2019.01490","DOI":"10.3389\/fmicb.2019.01490"},{"key":"ref9","doi-asserted-by":"crossref","unstructured":"Emerson S.U., Wagner R.R. Dissociation and reconstitution of the transcriptase and template activities of vesicular stomatitis B and T virions. J. Virol. 1972; 10(2): 297\u2013309. https:\/\/doi.org\/10.1128\/jvi.10.2.297-309.1972","DOI":"10.1128\/jvi.10.2.297-309.1972"},{"key":"ref10","doi-asserted-by":"crossref","unstructured":"Liang B., Li Z., Jenni S., Rahmeh A.A., Morin B.M., Grant T., et al. Structure of the L protein of vesicular stomatitis virus from electron cryomicroscopy. Cell. 2015; 162(2): 314\u201327. https:\/\/doi.org\/10.1016\/j.cell.2015.06.018","DOI":"10.1016\/j.cell.2015.06.018"},{"key":"ref11","doi-asserted-by":"crossref","unstructured":"Redondo N., Madan V., Alvarez E., Carrasco L. Impact of vesicular stomatitis virus M proteins on different cellular functions. PLoS One. 2015; 10(6): e0131137. https:\/\/doi.org\/10.1371\/journal.pone.0131137","DOI":"10.1371\/journal.pone.0131137"},{"key":"ref12","doi-asserted-by":"crossref","unstructured":"Carroll A.R., Wagner R.R. Role of the membrane (M) protein in endogenous inhibition of in vitro transcription by vesicular stomatitis virus. J. Virol. 1979; 29(1): 134\u201342. https:\/\/doi.org\/10.1128\/jvi.29.1.134-142.1979","DOI":"10.1128\/jvi.29.1.134-142.1979"},{"key":"ref13","doi-asserted-by":"crossref","unstructured":"Kim I.S., Jenni S., Stanifer M.L., Roth E., Whelan S.P., van Oijen A.M., et al. Mechanism of membrane fusion induced by vesicular stomatitis virus G protein. Proc. Natl Acad. Sci. USA. 2017; 114(1): E28\u201336. https:\/\/doi.org\/10.1073\/pnas.1618883114","DOI":"10.1073\/pnas.1618883114"},{"key":"ref14","doi-asserted-by":"crossref","unstructured":"Finkelshtein D., Werman A., Novick D., Barak S., Rubinstein M. LDL receptor and its family members serve as the cellular receptors for vesicular stomatitis virus. Proc. Natl Acad. Sci. USA. 2013; 110(18): 7306\u201311. https:\/\/doi.org\/10.1073\/pnas.1214441110","DOI":"10.1073\/pnas.1214441110"},{"key":"ref15","doi-asserted-by":"crossref","unstructured":"Liu G., Cao W., Salawudeen A., Zhu W., Emeterio K., Safronetz D., et al. Vesicular stomatitis virus: from agricultural pathogen to vaccine vector. Pathogens. 2021; 10(9): 1092. https:\/\/doi.org\/10.3390\/pathogens10091092","DOI":"10.3390\/pathogens10091092"},{"key":"ref16","doi-asserted-by":"crossref","unstructured":"Huang A.S., Palma E.L., Hewlett N., Roizman B. Pseudotype formation between enveloped RNA and DNA viruses. Nature. 1974; 252(5485): 743\u20135. https:\/\/doi.org\/10.1038\/252743a0","DOI":"10.1038\/252743a0"},{"key":"ref17","doi-asserted-by":"crossref","unstructured":"Salazar-Garc\u00eda M., Acosta-Contreras S., Rodr\u00edguez-Mart\u00ednez G., Cruz-Rangel A., Flores-Alanis A., Pati\u00f1o-L\u00f3pez G., et al. Pseudotyped vesicular stomatitis virus-severe acute respiratory syndrome-coronavirus-2 spike for the study of variants, vaccines, and therapeutics against coronavirus disease 2019. Front. Microbiol. 2022; 12: 817200. https:\/\/doi.org\/10.3389\/fmicb.2021.817200","DOI":"10.3389\/fmicb.2021.817200"},{"key":"ref18","doi-asserted-by":"crossref","unstructured":"Hanika A., Larisch B., Steinmann E., Schwegmann-We\u00dfels C., Herrler G., Zimmer G. Use of influenza C virus glycoprotein HEF for generation of vesicular stomatitis virus pseudotypes. J. Gen. Virol. 2005; 86(Pt. 5): 1455\u201365. https:\/\/doi.org\/10.1099\/vir.0.80788-0","DOI":"10.1099\/vir.0.80788-0"},{"key":"ref19","doi-asserted-by":"crossref","unstructured":"Takada A., Robison C., Goto H., Sanchez A., Murti K.G., Whitt M.A., et al. A system for functional analysis of Ebola virus glycoprotein. Proc. Natl Acad. Sci. USA. 1997; 94(26): 14764\u20139. https:\/\/doi.org\/10.1073\/pnas.94.26.14764","DOI":"10.1073\/pnas.94.26.14764"},{"key":"ref20","doi-asserted-by":"crossref","unstructured":"Steeds K., Hall Y., Slack G.S., Longet S., Strecker T., Fehling S.K., et al. Pseudotyping of VSV with Ebola virus glycoprotein is superior to HIV-1 for the assessment of neutralising antibodies. Sci. Rep. 2020; 10(1): 14289. https:\/\/doi.org\/10.1038\/s41598-020-71225-1","DOI":"10.1038\/s41598-020-71225-1"},{"key":"ref21","doi-asserted-by":"crossref","unstructured":"Thamamongood T., Jengarn J., Muangsanit P., Petpiroon N., Srisutthisamphan K., Attasombat K., et al. Pseudotyped zoonotic thogotoviruses exhibit broad entry range in mammalian cells. Virology. 2024; 589: 109914. https:\/\/doi.org\/10.1016\/j.virol.2023.109914","DOI":"10.1016\/j.virol.2023.109914"},{"key":"ref22","doi-asserted-by":"crossref","unstructured":"Suda Y., Fukushi S., Tani H., Murakami S., Saijo M., Horimoto T., et al. Analysis of the entry mechanism of Crimean-Congo hemorrhagic fever virus, using a vesicular stomatitis virus pseudotyping system. Arch. Virol. 2016; 161(6): 1447\u201354. https:\/\/doi.org\/10.1007\/s00705-016-2803-1","DOI":"10.1007\/s00705-016-2803-1"},{"key":"ref23","doi-asserted-by":"crossref","unstructured":"Santos-Ferreira N., Van Dycke J., Neyts J., Rocha-Pereira J. Current and future antiviral strategies to tackle gastrointestinal viral infections. Microorganisms. 2021; 9(8): 1599. https:\/\/doi.org\/10.3390\/microorganisms9081599","DOI":"10.3390\/microorganisms9081599"},{"key":"ref24","doi-asserted-by":"crossref","unstructured":"Ayoub P.G., Purkayastha A., Quintos J., Tam C., Lathrop L., Tam K., et al. Improved SARS-CoV-2 spike glycoproteins for pseudotyping lentiviral vectors. Front. Virol. 2021; 1: 793320. https:\/\/doi.org\/10.3389\/fviro.2021.793320","DOI":"10.3389\/fviro.2021.793320"},{"key":"ref25","doi-asserted-by":"crossref","unstructured":"Powell A.E., Xu D., Roth G.A., Zhang K., Chiu W., Appel E.A., et al. Multimerization of Ebola GP\u0394mucin on protein nanoparticle vaccines has minimal effect on elicitation of neutralizing antibodies. Front. Immunol. 2022; 13: 942897. https:\/\/doi.org\/10.3389\/fimmu.2022.942897","DOI":"10.3389\/fimmu.2022.942897"},{"key":"ref26","doi-asserted-by":"crossref","unstructured":"Douam F., Bobay L.M., Maurin G., Fresquet J., Calland N., Maisse C., et al. Specialization of hepatitis C virus envelope glycoproteins for B lymphocytes in chronically infected patients. J. Virol. 2015; 90(2): 992\u20131008. https:\/\/doi.org\/10.1128\/JVI.02516-15","DOI":"10.1128\/JVI.02516-15"},{"key":"ref27","doi-asserted-by":"crossref","unstructured":"Urbanowicz R.A., McClure C.P., King B., Mason C.P., Ball J.K., Tarr A.W. Novel functional hepatitis C virus glycoprotein isolates identified using an optimized viral pseudotype entry assay. J. Gen. Virol. 2016; 97(9): 2265\u201379. https:\/\/doi.org\/10.1099\/jgv.0.000537","DOI":"10.1099\/jgv.0.000537"},{"key":"ref28","doi-asserted-by":"crossref","unstructured":"Liu Q., Nie J., Huang W., Meng S., Yuan B., Gao D., et al. Comparison of two high-throughput assays for quantification of adenovirus type 5 neutralizing antibodies in a population of donors in China. PLoS One. 2012; 7(5): e37532. https:\/\/doi.org\/10.1371\/journal.pone.0037532","DOI":"10.1371\/journal.pone.0037532"},{"key":"ref29","doi-asserted-by":"crossref","unstructured":"Fujioka Y., Kashiwagi S., Yoshida A., Satoh A.O., Fujioka M., Amano M., et al. A method for the generation of pseudovirus particles bearing SARS coronavirus spike protein in high yields. Cell Struct. Funct. 2022; 47(1): 43\u201353. https:\/\/doi.org\/10.1247\/csf.21047","DOI":"10.1247\/csf.21047"},{"key":"ref30","doi-asserted-by":"crossref","unstructured":"Moroz V.D., Gasanov N.B., Egorov A.D., Malogolovkin A.S., Nagornykh M.O., Subcheva E.N., et al. A Method for the production of recombinant VSVs with confirmation of biological activity. Acta Naturae. 2024; 16(1): 59\u201366. https:\/\/doi.org\/10.32607\/actanaturae.27314","DOI":"10.32607\/actanaturae.27314"},{"key":"ref31","doi-asserted-by":"crossref","unstructured":"Li Q., Liu Q., Huang W., Li X., Wang Y. Current status on the development of pseudoviruses for enveloped viruses. Rev. Med. Virol. 2018; 28(1): e1963. https:\/\/doi.org\/10.1002\/rmv.1963","DOI":"10.1002\/rmv.1963"},{"key":"ref32","doi-asserted-by":"crossref","unstructured":"Xiang Q., Li L., Wu J., Tian M., Fu Y. Application of pseudovirus system in the development of vaccine, antiviral-drugs, and neutralizing antibodies. Microbiol. Res. 2022; 258: 126993. https:\/\/doi.org\/10.1016\/j.micres.2022.126993","DOI":"10.1016\/j.micres.2022.126993"},{"key":"ref33","doi-asserted-by":"crossref","unstructured":"Holguera J., Villar E., Mu\u00f1oz-Barroso I. Identification of cellular proteins that interact with Newcastle Disease Virus and human Respiratory Syncytial Virus by a two-dimensional virus overlay protein binding assay (VOPBA). Virus Res. 2014; 191: 138\u201342. https:\/\/doi.org\/10.1016\/j.virusres.2014.07.031","DOI":"10.1016\/j.virusres.2014.07.031"},{"key":"ref34","doi-asserted-by":"crossref","unstructured":"Rojek J.M., Spiropoulou C.F., Campbell K.P., Kunz S. Old World and clade C New World arenaviruses mimic the molecular mechanism of receptor recognition used by \u03b1-dystroglycan\u2019s host-derived ligands. J. Virol. 2007; 81(11): 5685\u201395. https:\/\/doi.org\/10.1128\/JVI.02574-06","DOI":"10.1128\/JVI.02574-06"},{"key":"ref35","doi-asserted-by":"crossref","unstructured":"Chan C.M., Chu H., Wang Y., Wong B.H., Zhao X., Zhou J., et al. Carcinoembryonic antigen-related cell adhesion molecule 5 is an important surface attachment factor that facilitates entry of middle east respiratory syndrome coronavirus. J. Virol. 2016; 90(20): 9114\u201327. https:\/\/doi.org\/10.1128\/JVI.01133-16","DOI":"10.1128\/JVI.01133-16"},{"key":"ref36","doi-asserted-by":"crossref","unstructured":"Xu Z.S., Du W.T., Wang S.Y., Wang M.Y., Yang Y.N., Li Y.H., et al. LDLR is an entry receptor for Crimean-Congo hemorrhagic fever virus. Cell Res. 2024; 34(2): 140\u201350. https:\/\/doi.org\/10.1038\/s41422-023-00917-w","DOI":"10.1038\/s41422-023-00917-w"},{"key":"ref37","doi-asserted-by":"crossref","unstructured":"Heuschkel M.J., Baumert T.F., Verrier E.R. Cell culture models for the study of hepatitis D virus entry and infection. Viruses. 2021; 13(8): 1532. https:\/\/doi.org\/10.3390\/v13081532","DOI":"10.3390\/v13081532"},{"key":"ref38","doi-asserted-by":"crossref","unstructured":"Horie H., Koike S., Kurata T., Sato-Yoshida Y., Ise I., Ota Y., et al. Transgenic mice carrying the human poliovirus receptor: new animal models for study of poliovirus neurovirulence. J. Virol. 1994; 68(2): 681\u20138. https:\/\/doi.org\/10.1128\/jvi.68.2.681-688.1994","DOI":"10.1128\/jvi.68.2.681-688.1994"},{"key":"ref39","doi-asserted-by":"crossref","unstructured":"Lu C.Y., Huang H.Y., Yang T.H., Chang L.Y., Lee C.Y., Huang L.M. siRNA silencing of angiotensin-converting enzyme 2 reduced severe acute respiratory syndrome-associated coronavirus replications in Vero E6 cells. Eur. J. Clin. Microbiol. Infect. Dis. 2008; 27(8): 709\u201315. https:\/\/doi.org\/10.1007\/s10096-008-0495-5","DOI":"10.1007\/s10096-008-0495-5"},{"key":"ref40","doi-asserted-by":"crossref","unstructured":"R\u00e9geard M., Trotard M., Lep\u00e8re C., Gripon P., Le Seyec J. Entry of pseudotyped hepatitis C virus into primary human hepatocytes depends on the scavenger class B type I receptor. J. Viral. Hepat. 2008; 15(12): 865\u201370. https:\/\/doi.org\/10.1111\/j.1365-2893.2008.01048.x","DOI":"10.1111\/j.1365-2893.2008.01048.x"},{"key":"ref41","doi-asserted-by":"crossref","unstructured":"Zhang H., Li Y., Wang H.B., Zhang A., Chen M.L., Fang Z.X., et al. Ephrin receptor A2 is an epithelial cell receptor for Epstein-Barr virus entry. Nat. Microbiol. 2018; 3(2): 1\u20138. https:\/\/doi.org\/10.1038\/s41564-017-0080-8","DOI":"10.1038\/s41564-017-0081-7"},{"key":"ref42","doi-asserted-by":"crossref","unstructured":"Shilagardi K., Spear E.D., Abraham R., Griffin D.E., Michaelis S. the integral membrane protein ZMPSTE24 protects cells from SARS-CoV-2 spike-mediated pseudovirus infection and syncytia formation. mBio. 2022; 13(5): e0254322. https:\/\/doi.org\/10.1128\/mbio.02543-22","DOI":"10.1128\/mbio.02543-22"},{"key":"ref43","doi-asserted-by":"crossref","unstructured":"Zhou Y.Q., Wang K., Wang X.Y., Cui H.Y., Zhao Y., Zhu P., et al. SARS-CoV-2 pseudovirus enters the host cells through spike protein-CD147 in an Arf6-dependent manner. Emerg. Microbes Infect. 2022; 11(1): 1135\u201344. https:\/\/doi.org\/10.1080\/22221751.2022.2059403","DOI":"10.1080\/22221751.2022.2059403"},{"key":"ref44","doi-asserted-by":"crossref","unstructured":"Zhao M.M., Yang W.L., Yang F.Y., Zhang L., Huang W.J., Hou W., et al. Cathepsin L plays a key role in SARS-CoV-2 infection in humans and humanized mice and is a promising target for new drug development. Signal Transduct. Target. Ther. 2021; 6(1): 134. https:\/\/doi.org\/10.1038\/s41392-021-00558-8","DOI":"10.1038\/s41392-021-00558-8"},{"key":"ref45","doi-asserted-by":"crossref","unstructured":"Tharkeshwar A.K., Trekker J., Vermeire W., Pauwels J., Sannerud R., Priestman D.A., et al. A novel approach to analyze lysosomal dysfunctions through subcellular proteomics and lipidomics: the case of NPC1 deficiency. Sci. Rep. 2017; 7: 41408. https:\/\/doi.org\/10.1038\/srep41408","DOI":"10.1038\/srep41408"},{"key":"ref46","doi-asserted-by":"crossref","unstructured":"Xiao J.H., Rijal P., Schimanski L., Tharkeshwar A.K., Wright E., Annaert W., et al. Characterization of influenza virus pseudotyped with Ebolavirus glycoprotein. J. Virol. 2018; 92(4): e00941\u201317. https:\/\/doi.org\/10.1128\/JVI.00941-17","DOI":"10.1128\/JVI.00941-17"},{"key":"ref47","doi-asserted-by":"crossref","unstructured":"Haft D.H., Selengut J., Mongodin E.F., Nelson K.E. A guild of 45 CRISPR-associated (Cas) protein families and multiple CRISPR\/Cas subtypes exist in prokaryotic genomes. PLoS Comput. Biol. 2005; 1(6): e60. https:\/\/doi.org\/10.1371\/journal.pcbi.0010060","DOI":"10.1371\/journal.pcbi.0010060"},{"key":"ref48","doi-asserted-by":"crossref","unstructured":"Jiang F., Doudna J.A. CRISPR\u2013Cas9 structures and mechanisms. Annu. Rev. Biophys. 2017; 46(1): 505\u201329. https:\/\/doi.org\/10.1146\/annurev-biophys-062215-010822","DOI":"10.1146\/annurev-biophys-062215-010822"},{"key":"ref49","doi-asserted-by":"crossref","unstructured":"Tani H., Iha K., Shimojima M., Fukushi S., Taniguchi S., Yoshikawa T., et al. Analysis of Lujo virus cell entry using pseudotype vesicular stomatitis virus. J. Virol. 2014; 88(13): 7317\u201330. https:\/\/doi.org\/10.1128\/JVI.00512-14","DOI":"10.1128\/JVI.00512-14"},{"key":"ref50","doi-asserted-by":"crossref","unstructured":"Li S., Ruan Z., Zhang H., Xu H. Recent achievements of bioluminescence imaging based on firefly luciferin-luciferase system. Eur. J. Med. Chem. 2021; 211: 113111. https:\/\/doi.org\/10.1016\/j.ejmech.2020.113111","DOI":"10.1016\/j.ejmech.2020.113111"},{"key":"ref51","doi-asserted-by":"crossref","unstructured":"Tani H. Analyses of entry mechanisms of novel emerging viruses using pseudotype VSV system. Trop. Med. Health. 2014; 42(2 Suppl.): 71\u201382. https:\/\/doi.org\/10.2149\/tmh.2014-S10","DOI":"10.2149\/tmh.2014-S10"},{"key":"ref52","doi-asserted-by":"crossref","unstructured":"Higa M.M., Petersen J., Hooper J., Doms R.W. Efficient production of Hantaan and Puumala pseudovirions for viral tropism and neutralization studies. Virology. 2012; 423(2): 134\u201342. https:\/\/doi.org\/10.1016\/j.virol.2011.08.012","DOI":"10.1016\/j.virol.2011.08.012"},{"key":"ref53","doi-asserted-by":"crossref","unstructured":"Matsuura Y., Tani H., Suzuki K., Kimura-Someya T., Suzuki R., Aizaki H., et al. Characterization of pseudotype VSV possessing HCV envelope proteins. Virology. 2001; 286(2): 263\u201375. https:\/\/doi.org\/10.1006\/viro.2001.0971","DOI":"10.1006\/viro.2001.0971"},{"key":"ref54","doi-asserted-by":"crossref","unstructured":"Tong W., Yin X.X., Lee B.J., Li Y.G. Preparation of vesicular stomatitis virus pseudotype with Chikungunya virus envelope protein. Acta Virol. 2015; 59(2): 189\u201393. https:\/\/doi.org\/10.4149\/av_2015_02_189","DOI":"10.4149\/av_2015_02_189"},{"key":"ref55","doi-asserted-by":"crossref","unstructured":"Sevilla N., Kunz S., Holz A., Lewicki H., Homann D., Yamada H., et al. Immunosuppression and resultant viral persistence by specific viral targeting of dendritic cells. J. Exp. Med. 2000; 192(9): 1249\u201360. https:\/\/doi.org\/10.1084\/jem.192.9.1249","DOI":"10.1084\/jem.192.9.1249"},{"key":"ref56","doi-asserted-by":"crossref","unstructured":"Millet J.K., Tang T., Nathan L., Jaimes J.A., Hsu H.L., Daniel S., et al. Production of pseudotyped particles to study highly pathogenic coronaviruses in a biosafety level 2 setting. J. Vis. Exp. 2019; (145): 10.3791\/59010. https:\/\/doi.org\/10.3791\/59010","DOI":"10.3791\/59010-v"}],"container-title":["Problems of Virology"],"original-title":[],"link":[{"URL":"https:\/\/virusjour.crie.ru\/jour\/article\/viewFile\/16829\/1074","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/virusjour.crie.ru\/jour\/article\/viewFile\/16829\/1074","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,4,3]],"date-time":"2026-04-03T14:36:48Z","timestamp":1775227008000},"score":1,"resource":{"primary":{"URL":"https:\/\/virusjour.crie.ru\/jour\/article\/view\/16829"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,2,28]]},"references-count":56,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2026,3,23]]}},"URL":"https:\/\/doi.org\/10.36233\/0507-4088-360","relation":{},"ISSN":["2411-2097","0507-4088"],"issn-type":[{"value":"2411-2097","type":"electronic"},{"value":"0507-4088","type":"print"}],"subject":[],"published":{"date-parts":[[2026,2,28]]}}}