{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T22:05:07Z","timestamp":1790028307678,"version":"4.0.1"},"reference-count":58,"publisher":"MDPI AG","issue":"2","license":[{"start":{"date-parts":[[2026,5,27]],"date-time":"2026-05-27T00:00:00Z","timestamp":1779840000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100002347","name":"Federal Ministry of Research, Technology and Space","doi-asserted-by":"publisher","award":["13FH048KX1"],"award-info":[{"award-number":["13FH048KX1"]}],"id":[{"id":"10.13039\/501100002347","id-type":"DOI","asserted-by":"publisher"}]},{"award":["13FH048KX1"],"award-info":[{"award-number":["13FH048KX1"]}],"id":[{"id":"https:\/\/ror.org\/04pz7b180","id-type":"ROR","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["BioTech"],"abstract":"<jats:p>Objectives: Membrane-enveloped virus-like particles (VLPs) constitute a versatile vaccine platform allowing for the display of heterologous viral surface antigens. The density of displayed antigens is paramount for the efficient elicitation of a strong cellular and humoral immune response. SARS-CoV-2 spike protein variants with engineered cytoplasmic tails (CTs) were generated to enhance decoration efficiency on the surface of VLPs formed by the HIV core protein Gag. These HIV (SARS-CoV-2) chimeric particles serve as a vaccine component prototype. Methods: Spike variants were first analyzed for cellular and surface expression as well as incorporation into extracellular vesicles (EVs) and VLPs using flow cytometric analysis and Western blot analysis. Receptor binding, fusogenicity, i.e., mediating the fusion of spike-positive with receptor-containing membranes, and the proteins\u2019 potential to mediate lentiviral vector gene transduction into susceptible target cells was examined by employing syncytia-formation assays and vector titration experiments. The display of a neutralization-sensitive epitope was examined utilizing immuno-precipitation using a neutralizing antibody. Results: All four variants were shown to be cell-surface expressed, to recruit the cognate receptor, to mediate membrane fusion and cell entry of lentiviral pseudotype vector particles and to decorate VLPs and EVs. However, the spike variant encompassing a truncated CT derived from the gibbon ape leukemia virus (GaLV) transmembrane (TM) envelope protein was most efficiently incorporated into HIV Gag-formed VLPs. All variants exposed a neutralization-sensitive epitope in the receptor binding domain. Conclusions: Engineering of the CTs of viral surface antigens can enhance VLP decoration, while required functionality of the ecto-domain such as receptor recognition, fusogenicity and neutralization-sensitive epitope presentation are not abrogated. This indicates the preservation of the structural integrity of the antigen required to elicit a neutralizing humoral immunity upon vaccination. The identified truncated CT of GaLV TM may be of utility to improve the incorporation of other viral surface antigens into a variety of membrane-enveloped VLPs derived from a range of different parental viruses.<\/jats:p>","DOI":"10.3390\/biotech15020038","type":"journal-article","created":{"date-parts":[[2026,5,27]],"date-time":"2026-05-27T14:36:56Z","timestamp":1779892616000},"page":"38","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Engineering Viral Surface Antigens to Improve Display on Virus-like Particle (VLP) Vaccine Prototypes"],"prefix":"10.3390","volume":"15","author":[{"given":"Mona","family":"Pi\u00dfarreck","sequence":"first","affiliation":[{"name":"Research Group Pharmaceutical Biotechnology, Faculty of Applied Natural Sciences, TH K\u00f6ln University of Applied Sciences, Campusplatz 1, 51379 Leverkusen, Germany"},{"name":"Institute of Biology, Faculty IV: School of Science and Technology, University of Siegen, 57068 Siegen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kristina","family":"Katsoutas","sequence":"additional","affiliation":[{"name":"Research Group Pharmaceutical Biotechnology, Faculty of Applied Natural Sciences, TH K\u00f6ln University of Applied Sciences, Campusplatz 1, 51379 Leverkusen, Germany"},{"name":"Institute of Biology, Faculty IV: School of Science and Technology, University of Siegen, 57068 Siegen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2211-786X","authenticated-orcid":false,"given":"J\u00f6rn","family":"Stitz","sequence":"additional","affiliation":[{"name":"Research Group Pharmaceutical Biotechnology, Faculty of Applied Natural Sciences, TH K\u00f6ln University of Applied Sciences, Campusplatz 1, 51379 Leverkusen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,5,27]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1038\/s41467-025-56118-z","article-title":"Recombinant expression systems for production of stabilised virus-like particles as next-generation polio vaccines","volume":"16","author":"Sherry","year":"2025","journal-title":"Nat. Commun."},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Han, T., Xiao, J., Zhang, S., Su, T., Liu, Y., and Zhang, Y. (2026). Research Progress Towards Poliovirus Virus-like Particle Vaccines: A Review. Vaccines, 14.","DOI":"10.3390\/vaccines14030216"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.semcancer.2013.11.002","article-title":"The human papillomavirus family and its role in carcinogenesis","volume":"26","author":"Tommasino","year":"2014","journal-title":"Semin. Cancer Biol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1038\/s41392-024-02083-w","article-title":"Roles of human papillomavirus in cancers: Oncogenic mechanisms and clinical use","volume":"10","author":"Zhang","year":"2025","journal-title":"Signal Transduct. Target. Ther."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"710","DOI":"10.1016\/j.jadohealth.2016.07.021","article-title":"Measuring Adolescent Human Papillomavirus Vaccine Coverage: A Match of Sexually Transmitted Disease Clinic and Immunization Registry Data","volume":"59","author":"Pathela","year":"2016","journal-title":"J. Adolesc. Health"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"4783","DOI":"10.1016\/j.vaccine.2018.02.087","article-title":"Can a single dose of human papillomavirus (HPV) vaccine prevent cervical cancer? Early findings from an Indian study","volume":"36","author":"Sankaranarayanan","year":"2018","journal-title":"Vaccine"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"100175","DOI":"10.1016\/j.pvr.2019.100175","article-title":"HPV genoprevalence and HPV knowledge in young women in Mongolia, five years following a pilot 4vHPV vaccination campaign","volume":"8","author":"Batmunkh","year":"2019","journal-title":"Papillomavirus Res."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"993","DOI":"10.1038\/s41423-022-00897-8","article-title":"Virus-like particle vaccinology, from bench to bedside","volume":"19","author":"Mohsen","year":"2022","journal-title":"Cell. Mol. Immunol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.virol.2022.01.008","article-title":"Components of a HIV-1 vaccine mediate virus-like particle (VLP)-formation and display of envelope proteins exposing broadly neutralizing epitopes","volume":"568","author":"Rosengarten","year":"2022","journal-title":"Virology"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1038\/s41541-025-01355-y","article-title":"Preclinical development of a cross-protective \u03b2-SARS-CoV-2 virus-like particle vaccine adjuvanted with MF59","volume":"11","author":"Earnest","year":"2026","journal-title":"npj Vaccines"},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Lee, S.-H., Chu, K.-B., Kim, M.-J., Mao, J., Eom, G.-D., Yoon, K.-W., Ahmed, M.A., and Quan, F.-S. (2023). Virus-like Particle Vaccine Expressing the Respiratory Syncytial Virus Pre-Fusion and G Proteins Confers Protection against RSV Challenge Infection. Pharmaceutics, 15.","DOI":"10.3390\/pharmaceutics15030782"},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Ross, T.M., Mahmood, K., Crevar, C.J., Schneider-Ohrum, K., Heaton, P.M., and Bright, R.A. (2009). A trivalent virus-like particle vaccine elicits protective immune responses against seasonal influenza strains in mice and ferrets. PLoS ONE, 4.","DOI":"10.1371\/journal.pone.0006032"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1007\/s12033-010-9268-3","article-title":"Trichoplusia ni cells (High Five) are highly efficient for the production of influenza A virus-like particles: A comparison of two insect cell lines as production platforms for influenza vaccines","volume":"45","author":"Krammer","year":"2010","journal-title":"Mol. Biotechnol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/0092-8674(89)90873-8","article-title":"Assembly and release of HIV-1 precursor Pr55gag virus-like particles from recombinant baculovirus-infected insect cells","volume":"59","author":"Gheysen","year":"1989","journal-title":"Cell"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"592","DOI":"10.1016\/j.chom.2008.10.013","article-title":"Three-dimensional analysis of budding sites and released virus suggests a revised model for HIV-1 morphogenesis","volume":"4","author":"Carlson","year":"2008","journal-title":"Cell Host Microbe"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"2660","DOI":"10.1002\/bit.27786","article-title":"Characterization of HIV-1 virus-like particles and determination of Gag stoichiometry for different production platforms","volume":"118","author":"Jorge","year":"2021","journal-title":"Biotechnol. Bioeng."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"13925","DOI":"10.1073\/pnas.241320298","article-title":"Plasma membrane rafts play a critical role in HIV-1 assembly and release","volume":"98","author":"Ono","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"9749","DOI":"10.1128\/JVI.00743-11","article-title":"Gag induces the coalescence of clustered lipid rafts and tetraspanin-enriched microdomains at HIV-1 assembly sites on the plasma membrane","volume":"85","author":"Hogue","year":"2011","journal-title":"J. Virol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1029","DOI":"10.1042\/BST20180019","article-title":"Inside job: How the ESCRTs release HIV-1 from infected cells","volume":"46","author":"Hurley","year":"2018","journal-title":"Biochem. Soc. Trans."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/j.cell.2020.02.052","article-title":"SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor","volume":"181","author":"Hoffmann","year":"2020","journal-title":"Cell"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"1620","DOI":"10.1038\/s41467-020-15562-9","article-title":"Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV","volume":"11","author":"Ou","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"4146","DOI":"10.1073\/pnas.1200448109","article-title":"Formation and release of arrestin domain-containing protein 1-mediated microvesicles (ARMMs) at plasma membrane by recruitment of TSG101 protein","volume":"109","author":"Nabhan","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1038\/bjc.2017.18","article-title":"Exosomes confer chemoresistance to pancreatic cancer cells by promoting ROS detoxification and miR-155-mediated suppression of key gemcitabine-metabolising enzyme, DCK","volume":"116","author":"Patel","year":"2017","journal-title":"Br. J. Cancer"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1083\/jcb.201211138","article-title":"Extracellular vesicles: Exosomes, microvesicles, and friends","volume":"200","author":"Raposo","year":"2013","journal-title":"J. Cell Biol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1016\/j.jviromet.2012.01.003","article-title":"Purification of norovirus-like particles (VLPs) by ion exchange chromatography","volume":"181","author":"Koho","year":"2012","journal-title":"J. Virol. Methods"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/j.chroma.2016.12.085","article-title":"Quantification and characterization of virus-like particles by size-exclusion chromatography and nanoparticle tracking analysis","volume":"1487","author":"Steppert","year":"2017","journal-title":"J. Chromatogr. A"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"14","DOI":"10.56530\/lcgc.int.gp3972j6","article-title":"Challenges in the Analytical Characterization of VLPs Through HPLC-Based Methods","volume":"1","author":"Rathore","year":"2024","journal-title":"LCGC Int."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"124539","DOI":"10.1016\/j.jchromb.2025.124539","article-title":"Optimizing nuclease treatment to enhance anion exchange chromatography of HIV-derived virus-like particles","volume":"1256","author":"Taft","year":"2025","journal-title":"J. Chromatogr. B Anal. Technol. Biomed. Life Sci."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1448","DOI":"10.1126\/science.8248784","article-title":"The influence of antigen organization on B cell responsiveness","volume":"262","author":"Bachmann","year":"1993","journal-title":"Science"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"548","DOI":"10.1016\/j.immuni.2020.08.001","article-title":"Multifaceted Effects of Antigen Valency on B Cell Response Composition and Differentiation In Vivo","volume":"53","author":"Kato","year":"2020","journal-title":"Immunity"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"3671","DOI":"10.1073\/pnas.73.10.3671","article-title":"Molecular determinants of immunogenicity: The immunon model of immune response","volume":"73","author":"Dintzis","year":"1976","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1006\/viro.1997.8669","article-title":"Increased incorporation of chimeric human immunodeficiency virus type 1 gp120 proteins into Pr55gag virus-like particles by an Epstein-Barr virus gp220\/350-derived transmembrane domain","volume":"235","author":"Deml","year":"1997","journal-title":"Virology"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"10869","DOI":"10.1128\/JVI.00542-07","article-title":"Incorporation of high levels of chimeric human immunodeficiency virus envelope glycoproteins into virus-like particles","volume":"81","author":"Wang","year":"2007","journal-title":"J. Virol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/j.virol.2015.09.015","article-title":"Effects of modification of the HIV-1 Env cytoplasmic tail on immunogenicity of VLP vaccines","volume":"489","author":"Vzorov","year":"2016","journal-title":"Virology"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1110","DOI":"10.1128\/JVI.01062-20","article-title":"Optimized Pseudotyping Conditions for the SARS-COV-2 Spike Glycoprotein","volume":"94","author":"Johnson","year":"2020","journal-title":"J. Virol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"e20201181","DOI":"10.1084\/jem.20201181","article-title":"Measuring SARS-CoV-2 neutralizing antibody activity using pseudotyped and chimeric viruses","volume":"217","author":"Schmidt","year":"2020","journal-title":"J. Exp. Med."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"5783","DOI":"10.1002\/j.1460-2075.1996.tb00964.x","article-title":"Direct interaction between the envelope and matrix proteins of HIV-1","volume":"15","author":"Cosson","year":"1996","journal-title":"EMBO J."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"6583","DOI":"10.1128\/JVI.00600-16","article-title":"HIV-1 Gag, Envelope, and Extracellular Determinants Cooperate to Regulate the Stability and Turnover of Virological Synapses","volume":"90","author":"Gardiner","year":"2016","journal-title":"J. Virol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1073\/pnas.97.1.343","article-title":"The long cytoplasmic tail of gp41 is required in a cell type-dependent manner for HIV-1 envelope glycoprotein incorporation into virions","volume":"97","author":"Murakami","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1133","DOI":"10.1038\/gt.2011.206","article-title":"Development of the Nanobody display technology to target lentiviral vectors to antigen-presenting cells","volume":"19","author":"Goyvaerts","year":"2012","journal-title":"Gene Ther."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"2241","DOI":"10.1099\/0022-1317-83-9-2241","article-title":"Identification of R-peptides in envelope proteins of C-type retroviruses","volume":"83","author":"Bobkova","year":"2002","journal-title":"J. Gen. Virol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1577","DOI":"10.1099\/vir.0.81231-0","article-title":"Envelope proteins of spleen necrosis virus form infectious human immunodeficiency virus type 1 pseudotype vector particles, but fail to incorporate upon substitution of the cytoplasmic domain with that of Gibbon ape leukemia virus","volume":"87","author":"Stitz","year":"2006","journal-title":"J. Gen. Virol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1016\/j.virol.2022.09.008","article-title":"Ecotropic HIV-1 vectors pseudotyped with R-peptide-deleted envelope protein variants reveal improved gene transfer efficiencies","volume":"577","author":"Tschorn","year":"2022","journal-title":"Virology"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.virol.2019.02.014","article-title":"Rapid establishment of stable retroviral packaging cells and recombinant susceptible target cell lines employing novel transposon vectors derived from Sleeping Beauty","volume":"531","author":"Berg","year":"2019","journal-title":"Virology"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"102170","DOI":"10.1016\/j.isci.2021.102170","article-title":"Quantitative assays reveal cell fusion at minimal levels of SARS-CoV-2 spike protein and fusion from without","volume":"24","author":"Theuerkauf","year":"2021","journal-title":"iScience"},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"van Heuvel, Y., Schatz, S., Hein, M., Dogra, T., Kazenmaier, D., Tschorn, N., Genzel, Y., and Stitz, J. (2023). Novel suspension retroviral packaging cells generated by transposition using transposase encoding mRNA advance vector yields and enable production in bioreactors. Front. Bioeng. Biotechnol., 11.","DOI":"10.3389\/fbioe.2023.1076524"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1007\/978-1-4939-9853-1_20","article-title":"Advanced Establishment of Stable Recombinant Human Suspension Cell Lines Using Genotype-Phenotype Coupling Transposon Vectors","volume":"2070","author":"Berg","year":"2020","journal-title":"Methods Mol. Biol."},{"key":"ref_48","first-page":"12.10.1","article-title":"Production and titration of lentiviral vectors","volume":"54","author":"Salmon","year":"2007","journal-title":"Curr. Protoc. Hum. Genet."},{"key":"ref_49","doi-asserted-by":"crossref","unstructured":"Rosengarten, J.F., Schatz, S., and Stitz, J. (2022). Detection of Neutralization-sensitive Epitopes in Antigens Displayed on Virus-Like Particle (VLP)-Based Vaccines Using a Capture Assay. J. Vis. Exp., e63137.","DOI":"10.3791\/63137-v"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"e0158525","DOI":"10.1128\/jvi.01585-25","article-title":"Characterization of full-length and cytoplasmic tail-truncated envelope glycoproteins incorporated into human immunodeficiency virus (HIV-1) virions and virus-like particles","volume":"99","author":"Anang","year":"2025","journal-title":"J. Virol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"1350","DOI":"10.1128\/JVI.73.2.1350-1361.1999","article-title":"Interactions of the cytoplasmic domains of human and simian retroviral transmembrane proteins with components of the clathrin adaptor complexes modulate intracellular and cell surface expression of envelope glycoproteins","volume":"73","author":"Shacklett","year":"1999","journal-title":"J. Virol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"15773","DOI":"10.1074\/jbc.273.25.15773","article-title":"A membrane-proximal tyrosine-based signal mediates internalization of the HIV-1 envelope glycoprotein via interaction with the AP-2 clathrin adaptor","volume":"273","author":"Boge","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"414","DOI":"10.1091\/mbc.e06-06-0535","article-title":"A conserved dileucine motif mediates clathrin and AP-2-dependent endocytosis of the HIV-1 envelope protein","volume":"18","author":"Byland","year":"2007","journal-title":"Mol. Biol. Cell"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"2982","DOI":"10.1128\/JVI.75.6.2982-2992.2001","article-title":"The highly conserved C-terminal dileucine motif in the cytosolic domain of the human immunodeficiency virus type 1 envelope glycoprotein is critical for its association with the AP-1 clathrin adaptor correction of adapter","volume":"75","author":"Wyss","year":"2001","journal-title":"J. Virol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1006\/viro.1997.8839","article-title":"Interaction of endocytic signals from the HIV-1 envelope glycoprotein complex with members of the adaptor medium chain family","volume":"238","author":"Ohno","year":"1997","journal-title":"Virology"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1126\/science.abc5902","article-title":"Potent neutralizing antibodies from COVID-19 patients define multiple targets of vulnerability","volume":"369","author":"Brouwer","year":"2020","journal-title":"Science"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"1422","DOI":"10.1038\/s41591-020-0998-x","article-title":"Rapid isolation and profiling of a diverse panel of human monoclonal antibodies targeting the SARS-CoV-2 spike protein","volume":"26","author":"Zost","year":"2020","journal-title":"Nat. Med."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1695","DOI":"10.1038\/s41598-017-01739-8","article-title":"Extracellular Vesicles Carry HIV Env and Facilitate Hiv Infection of Human Lymphoid Tissue","volume":"7","author":"Arakelyan","year":"2017","journal-title":"Sci. Rep."}],"container-title":["BioTech"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2673-6284\/15\/2\/38\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,5,27]],"date-time":"2026-05-27T15:03:45Z","timestamp":1779894225000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2673-6284\/15\/2\/38"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,5,27]]},"references-count":58,"journal-issue":{"issue":"2","published-online":{"date-parts":[[2026,6]]}},"alternative-id":["biotech15020038"],"URL":"https:\/\/doi.org\/10.3390\/biotech15020038","relation":{},"ISSN":["2673-6284"],"issn-type":[{"value":"2673-6284","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,5,27]]}}}