Sequences of the peptides synthetized for each protein
Protein
Peptide number
Sequence
Peptide length (amino acids)
Gp350/220
11382
142HHAEMQNPVYLIPETVPYIK161
20
11389
282YVFYSGNGPKASGGDYCIQS301
20
Gp85 [glycoprotein H (gH)]
11416
822PSTSSKLRPRWTFTSPPVTTY841
21
11435
181TYKRVTEKGDEHVLSLVFGK200
20
11436
201TKDLPDLRGPFSYPSLTSAQ220
20
11438
241YFVPNLKDMFSRAVTMTAAS260
20
BNRF1/p140
11465
101GTESALEASGNNYVYAYGPD120
20
11521
1221YVLQNAHQIACHFHSNGTDA1240
20
Declarations
Acknowledgments
The authors would like to express their sincere gratitude to the Universidad Nacional de Colombia for its continuous support and encouragement in fostering scientific research and innovation. We express our deepest gratitude to Prof. Manuel E. Patarroyo, whose invaluable guidance and mentorship were instrumental in shaping the research review described here. Sadly, Prof. Manuel E. Patarroyo passed away on January 9, 2025, during the preparation of this manuscript. His dedication to scientific inquiry and his profound impact on the field will always be remembered. Molecular graphics and analyses performed with PyMOL.
Author contributions
DPJ: Conceptualization, Investigation, Writing—original draft, Writing—review & editing. FGQ: Conceptualization, Investigation. MUM: Conceptualization, Validation, Writing—review & editing, Supervision. All authors read and approved the submitted version.
Conflicts of interest
Fanny Guzmán-Quimbayo who is the Guest Editor of Exploration of Drug Science had no involvement in the decision-making or the review process of this manuscript. The other authors declare that they have no conflicts of interest.
Ethical approval
Not applicable.
Consent to participate
Not applicable.
Consent to publication
Not applicable.
Availability of data and materials
The dataset analyzed for this study can be found in the RCSB Protein Data Bank RCSB PDB: Homepage.
Open Exploration maintains a neutral stance on jurisdictional claims in published institutional affiliations and maps. All opinions expressed in this article are the personal views of the author(s) and do not represent the stance of the editorial team or the publisher.
References
Rowles DL, Terhune SS, Cristea IM. Discovery of host–viral protein complexes during infection.Methods Mol Biol. 2013;1064:43–70. [DOI] [PubMed] [PMC]
Yang M, Sunderland K, Mao C. Virus-Derived Peptides for Clinical Applications.Chem Rev. 2017;117:10377–402. [DOI] [PubMed] [PMC]
Trier N, Hansen P, Houen G. Peptides, Antibodies, Peptide Antibodies and More.Int J Mol Sci. 2019;20:6289. [DOI] [PubMed] [PMC]
Al-Azzam S, Ding Y, Liu J, Pandya P, Ting JP, Afshar S. Peptides to combat viral infectious diseases.Peptides. 2020;134:170402. [DOI] [PubMed] [PMC]
Kim J, Cho BH, Jang YS. Understanding the Roles of Host Defense Peptides in Immune Modulation: From Antimicrobial Action to Potential as Adjuvants.J Microbiol Biotechnol. 2023;33:288–98. [DOI] [PubMed] [PMC]
Polaris Observatory HCV Collaborators. Global change in hepatitis C virus prevalence and cascade of care between 2015 and 2020: a modelling study.Lancet Gastroenterol Hepatol. 2022;7:396–415. [DOI] [PubMed]
de Melo Silva J, Pinheiro-Silva R, Dhyani A, Pontes GS. Cytomegalovirus and Epstein-Barr Infections: Prevalence and Impact on Patients with Hematological Diseases.Biomed Res Int. 2020;2020:1627824. [DOI] [PubMed] [PMC]
Kombe Kombe AJ, Li B, Zahid A, Mengist HM, Bounda GA, Zhou Y, et al. Epidemiology and Burden of Human Papillomavirus and Related Diseases, Molecular Pathogenesis, and Vaccine Evaluation.Front Public Health. 2021;8:552028. [DOI] [PubMed] [PMC]
Galati L, Chiantore MV, Marinaro M, Di Bonito P. Human Oncogenic Viruses: Characteristics and Prevention Strategies—Lessons Learned from Human Papillomaviruses.Viruses. 2024;16:416. [DOI] [PubMed] [PMC]
Chen CJ, You SL, Hsu WL, Yang HI, Lee MH, Chen HC, et al. Epidemiology of Virus Infection and Human Cancer.Recent Results Cancer Res. 2021;217:13–45. [DOI] [PubMed]
Schiffman M, Doorbar J, Wentzensen N, de Sanjosé S, Fakhry C, Monk BJ, et al. Carcinogenic human papillomavirus infection.Nat Rev Dis Primers. 2016;2:16086. [DOI] [PubMed]
Lemon SM, McGivern DR. Is hepatitis C virus carcinogenic?Gastroenterology. 2012;142:1274–8. [DOI] [PubMed] [PMC]
Young LS, Murray PG. Epstein–Barr virus and oncogenesis: from latent genes to tumours.Oncogene. 2003;22:5108–21. [DOI] [PubMed]
Hashemi S, Vosough P, Taghizadeh S, Savardashtaki A. Therapeutic peptide development revolutionized: Harnessing the power of artificial intelligence for drug discovery.Heliyon. 2024;10:e40265. [DOI] [PubMed] [PMC]
Han Y, Wu F, Zhang Y, Liu J, Wu Y, Wang Y, et al. Structure-based design of antibodies targeting the EBNA1 DNA-binding domain to block Epstein–Barr virus latent infection and tumor growth.MedComm (2020). 2024;5:e739. [DOI] [PubMed] [PMC]
Fénéant L, Levy S, Cocquerel L. CD81 and hepatitis C virus (HCV) infection.Viruses. 2014;6:535–72. [DOI] [PubMed] [PMC]
Elfiky AA, Saied HR, Ali MA. Targeting of HPV E6 at the binding sites to the host-cell E6AP, p53, and the endoplasmic reticulum-resident chaperone, GRP78.J Biomol Struct Dyn. 2024;42:12385–95. [DOI] [PubMed]
Naughton P, Enright F, Lucey B. Infectious mononucleosis: new concepts in clinical presentation, epidemiology, and host response.Curr Opin Infect Dis. 2024;37:157–63. [DOI] [PubMed]
Thompson MP, Kurzrock R. Epstein-Barr virus and cancer.Clin Cancer Res. 2004;10:803–21. [DOI] [PubMed]
Bakkalci D, Jia Y, Winter JR, Lewis JE, Taylor GS, Stagg HR. Risk factors for Epstein Barr virus-associated cancers: a systematic review, critical appraisal, and mapping of the epidemiological evidence.J Glob Health. 2020;10:010405. [DOI] [PubMed] [PMC]
Chakravorty S, Afzali B, Kazemian M. EBV-associated diseases: Current therapeutics and emerging technologies.Front Immunol. 2022;13:1059133. [DOI] [PubMed] [PMC]
Santamaria H, Manoutcharian K, Rocha L, Gonzalez E, Acero G, Govezensky T, et al. Identification of peptide sequences specific for serum antibodies from human papillomavirus-infected patients using phage display libraries.Clin Immunol. 2001;101:296–302. [DOI] [PubMed]
Shannon-Lowe C, Rickinson A. The Global Landscape of EBV-Associated Tumors.Front Oncol. 2019;9:713. [DOI] [PubMed] [PMC]
Naseem M, Barzi A, Brezden-Masley C, Puccini A, Berger MD, Tokunaga R, et al. Outlooks on Epstein-Barr virus associated gastric cancer.Cancer Treat Rev. 2018;66:15–22. [DOI] [PubMed] [PMC]
Zeng ZM, Luo FF, Zou LX, He RQ, Pan DH, Chen X, et al. Human papillomavirus as a potential risk factor for gastric cancer: a meta-analysis of 1,917 cases.Onco Targets Ther. 2016;9:7105–14. [DOI] [PubMed] [PMC]
Bae J. Human papillomavirus infection and gastric cancer risk: A meta-epidemiological review.World J Virol. 2021;10:209–16. [DOI] [PubMed] [PMC]
Stasi C, Silvestri C, Voller F. Update on Hepatitis C Epidemiology: Unaware and Untreated Infected Population Could Be the Key to Elimination.SN Compr Clin Med. 2020;2:2808–15. [DOI] [PubMed] [PMC]
Axley P, Ahmed Z, Ravi S, Singal AK. Hepatitis C Virus and Hepatocellular Carcinoma: A Narrative Review.J Clin Transl Hepatol. 2018;6:79–84. [DOI] [PubMed] [PMC]
Roger S, Ducancelle A, Le Guillou-Guillemette H, Gaudy C, Lunel F. HCV virology and diagnosis.Clin Res Hepatol Gastroenterol. 2021;45:101626. [DOI] [PubMed]
Yao QY, Rickinson AB, Epstein MA. A re-examination of the Epstein-Barr virus carrier state in healthy seropositive individuals.Int J Cancer. 1985;35:35–42. [DOI] [PubMed]
Hong J, Zhong L, Zheng Q, Wu Q, Zha Z, Wei D, et al. A Neutralizing Antibody Targeting gH Provides Potent Protection against EBV Challenge In Vivo.J Virol. 2022;96:e0007522. [DOI] [PubMed] [PMC]
Massini G, Siemer D, Hohaus S. EBV in Hodgkin Lymphoma.Mediterr J Hematol Infect Dis. 2009;1:e2009013. [PubMed] [PMC]
Shinozaki-Ushiku A, Kunita A, Fukayama M. Update on Epstein-Barr virus and gastric cancer (review).Int J Oncol. 2015;46:1421–34. [DOI] [PubMed]
Volaric AK, Fedoriw Y. Epstein-Barr virus-associated B-cell lymphoproliferative disorders and lymphomas: Diagnostic overlaps and defining features.Hum Pathol. 2024;105697. [DOI] [PubMed]
El-Mallawany NK, Rouce RH. EBV and post-transplant lymphoproliferative disorder: a complex relationship.Hematology Am Soc Hematol Educ Program. 2024;2024:728–35. [DOI] [PubMed] [PMC]
Lossius A, Johansen JN, Torkildsen Ø, Vartdal F, Holmøy T. Epstein-Barr virus in systemic lupus erythematosus, rheumatoid arthritis and multiple sclerosis—association and causation.Viruses. 2012;4:3701–30. [DOI] [PubMed] [PMC]
Posnett DN. Herpesviruses and autoimmunity.Curr Opin Investig Drugs. 2008;9:505–14. [PubMed]
Wong Y, Meehan MT, Burrows SR, Doolan DL, Miles JJ. Estimating the global burden of Epstein–Barr virus-related cancers.J Cancer Res Clin Oncol. 2022;148:31–46. [DOI] [PubMed] [PMC]
Bu GL, Xie C, Kang YF, Zeng MS, Sun C. How EBV Infects: The Tropism and Underlying Molecular Mechanism for Viral Infection.Viruses. 2022;14:2372. [DOI] [PubMed] [PMC]
Connolly SA, Jackson JO, Jardetzky TS, Longnecker R. Fusing structure and function: a structural view of the herpesvirus entry machinery.Nat Rev Microbiol. 2011;9:369–81. [DOI] [PubMed] [PMC]
Chen J, Longnecker R. Epithelial cell infection by Epstein–Barr virus.FEMS Microbiol Rev. 2019;43:674–83. [DOI] [PubMed] [PMC]
Cui X, Cao Z, Ishikawa Y, Cui S, Imadome KI, Snapper CM. Immunization with Epstein-Barr Virus Core Fusion Machinery Envelope Proteins Elicit High Titers of Neutralizing Activities and Protect Humanized Mice from Lethal Dose EBV Challenge.Vaccines (Basel). 2021;9:285. [DOI] [PubMed] [PMC]
Stampfer SD, Heldwein EE. Stuck in the middle: structural insights into the role of the gH/gL heterodimer in herpesvirus entry.Curr Opin Virol. 2013;3:13–9. [DOI] [PubMed] [PMC]
Möhl BS, Chen J, Park SJ, Jardetzky TS, Longnecker R. Epstein-Barr Virus Fusion with Epithelial Cells Triggered by gB Is Restricted by a gL Glycosylation Site.J Virol. 2017;91:e01255–17. [DOI] [PubMed] [PMC]
Möhl BS, Chen J, Sathiyamoorthy K, Jardetzky TS, Longnecker R. Structural and Mechanistic Insights into the Tropism of Epstein-Barr Virus.Mol Cells. 2016;39:286–91. [DOI] [PubMed] [PMC]
Li Q, Turk SM, Hutt-Fletcher LM. The Epstein-Barr virus (EBV) BZLF2 gene product associates with the gH and gL homologs of EBV and carries an epitope critical to infection of B cells but not of epithelial cells.J Virol. 1995;69:3987–94. [DOI] [PubMed] [PMC]
Connolly SA, Jardetzky TS, Longnecker R. The structural basis of herpesvirus entry.Nat Rev Microbiol. 2021;19:110–21. [DOI] [PubMed] [PMC]
Wang X, Kenyon WJ, Li Q, Müllberg J, Hutt-Fletcher LM. Epstein-Barr virus uses different complexes of glycoproteins gH and gL to infect B lymphocytes and epithelial cells.J Virol. 1998;72:5552–8. [DOI] [PubMed] [PMC]
Silva JM, Alves CEC, Pontes GS. Epstein-Barr virus: the mastermind of immune chaos.Front Immunol. 2024;15:1297994. [DOI] [PubMed] [PMC]
Urquiza M, Suarez J, Lopez R, Vega E, Patino H, Garcia J, et al. Identifying gp85-regions involved in Epstein–Barr virus binding to B-lymphocytes.Biochem Biophys Res Commun. 2004;319:221–9. [DOI] [PubMed]
Zhu Q, Shan S, Yu J, Wang X, Zhang L, Zeng M. Crystal structure of EBV gH/gL bound with neutralizing antibody 1D8 [Internet].wwPDB [cited 2025 Jan 20]. Available from: https://doi.org/10.2210/pdb7d5z/pdb
The PyMOL Molecular Graphics System (Version 1.2r3pre) [Software]. Schrödinger, LLC.; [cited 2025 Jan 30]. Available from: https://www.pymol.org/
Fang XY, Zhao GX, Zeng MS, Liu Z. Cryo-EM structure of EBV gH/gL-gp42 in complex with fab 2C1 [Internet].wwPDB [cited 2025 Jan 30]. Available from: https://doi.org/10.2210/pdb8khr/pdb
Tanner J, Weis J, Fearon D, Whang Y, Kieff E. Epstein-Barr virus gp350/220 binding to the B lymphocyte C3d receptor mediates adsorption, capping, and endocytosis.Cell. 1987;50:203–13. [DOI] [PubMed]
Persson Berg L, Thomsson E, Hasi G, Bäckström M, Bergström T. Recombinant Epstein-Barr virus glycoprotein 350 as a serological antigen.J Virol Methods. 2020;284:113927. [DOI] [PubMed]
Young KA, Chen XS, Holers VM, Hannan JP. Isolating the Epstein-Barr virus gp350/220 binding site on complement receptor type 2 (CR2/CD21).J Biol Chem. 2007;282:36614–25. [DOI] [PubMed]
Nemerow GR, Houghten RA, Moore MD, Cooper NR. Identification of an epitope in the major envelope protein of Epstein-Barr virus that mediates viral binding to the B lymphocyte EBV receptor (CR2).Cell. 1989;56:369–77. [DOI] [PubMed]
Zeng C, Qiao M, Chen Y, Xie H. EBV-positive glycoproteins associated with nasopharyngeal carcinoma.Pathol Res Pract. 2024;260:155427. [DOI] [PubMed]
Joyce MG, Bu W, Chen WH, Gillespie RA, Andrews SF, Wheatley AK, et al. Structural basis for complement receptor engagement and virus neutralization through Epstein-Barr virus gp350.Immunity. 2025;58:295–308.e5. [DOI] [PubMed]
D’Addario M, Libermann TA, Xu J, Ahmad A, Menezes J. Epstein-Barr virus and its glycoprotein-350 upregulate IL-6 in human B-lymphocytes via CD21, involving activation of NF-κB and different signaling pathways.J Mol Biol. 2001;308:501–14. [DOI] [PubMed]
Aliyu M, Zohora FT, Anka AU, Ali K, Maleknia S, Saffarioun M, et al. Interleukin-6 cytokine: An overview of the immune regulation, immune dysregulation, and therapeutic approach.Int Immunopharmacol. 2022;111:109130. [DOI] [PubMed]
Zhang G, Tsang CM, Deng W, Yip YL, Lui VW, Wong SC, et al. Enhanced IL-6/IL-6R signaling promotes growth and malignant properties in EBV-infected premalignant and cancerous nasopharyngeal epithelial cells.PLoS One. 2013;8:e62284. [DOI] [PubMed] [PMC]
Rösen-Wolff A. Epstein-Barr-Virus. In: Darai G, Handermann M, Sonntag HG, Tidona CA, Zöller L, editors. Lexikon der Infektionskrankheiten des Menschen. Berlin, Heidelberg: Springer; 2009. pp. 292–5.
Kempkes B, Robertson ES. Epstein-Barr virus latency: current and future perspectives.Curr Opin Virol. 2015;14:138–44. [DOI] [PubMed] [PMC]
Oliveira LOD, Costa IB, Quaresma JAS. Association between Epstein-Barr virus LMP-1 and Hodgkin lymphoma LMP-1 mechanisms in Hodgkin lymphoma development.Rev Med Virol. 2024;34:e2561. [DOI] [PubMed]
Gholiha AR, Hollander P, Glimelius I, Hedstrom G, Molin D, Hjalgrim H, et al. Revisiting IL-6 expression in the tumor microenvironment of classical Hodgkin lymphoma.Blood Adv. 2021;5:1671–81. [DOI] [PubMed] [PMC]
Sueur C, Lupo J, Mas P, Morand P, Boyer V. Difference in cytokine production and cell cycle progression induced by Epstein-Barr virus Lmp1 deletion variants in Kmh2, a Hodgkin lymphoma cell line.Virol J. 2014;11:94. [DOI] [PubMed] [PMC]
Hatton OL, Harris-Arnold A, Schaffert S, Krams SM, Martinez OM. The interplay between Epstein–Barr virus and B lymphocytes: implications for infection, immunity, and disease.Immunol Res. 2014;58:268–76. [DOI] [PubMed] [PMC]
Damania B, Kenney SC, Raab-Traub N. Epstein-Barr virus: Biology and clinical disease.Cell. 2022;185:3652–70. [DOI] [PubMed] [PMC]
Yiu SPT, Guo R, Zerbe C, Weekes MP, Gewurz BE. Epstein-Barr virus BNRF1 destabilizes SMC5/6 cohesin complexes to evade its restriction of replication compartments.Cell Rep. 2022;38:110411. [DOI] [PubMed] [PMC]
Tsai K, Chan L, Gibeault R, Conn K, Dheekollu J, Domsic J, et al. Viral reprogramming of the Daxx histone H3.3 chaperone during early Epstein-Barr virus infection.J Virol. 2014;88:14350–63. [DOI] [PubMed] [PMC]
Tsai K, Thikmyanova N, Wojcechowskyj JA, Delecluse HJ, Lieberman PM. EBV tegument protein BNRF1 disrupts DAXX-ATRX to activate viral early gene transcription.PLoS Pathog. 2011;7:e1002376. [DOI] [PubMed] [PMC]
Edson CM, Thorley-Lawson DA. Epstein-Barr virus membrane antigens: characterization, distribution, and strain differences.J Virol. 1981;39:172–84. [DOI] [PubMed] [PMC]
Johannsen E, Luftig M, Chase MR, Weicksel S, Cahir-McFarland E, Illanes D, et al. Proteins of purified Epstein-Barr virus.Proc Natl Acad Sci U S A. 2004;101:16286–91. [DOI] [PubMed] [PMC]
Cui X, Cao Z, Wang S, Lee RB, Wang X, Murata H, et al. Novel trimeric human cytomegalovirus glycoprotein B elicits a high-titer neutralizing antibody response.Vaccine. 2018;36:5580–90. [DOI] [PubMed] [PMC]
Diamond DJ, La Rosa C, Chiuppesi F, Contreras H, Dadwal S, Wussow F, et al. A fifty-year odyssey: prospects for a cytomegalovirus vaccine in transplant and congenital infection.Expert Rev Vaccines. 2018;17:889–911. [DOI] [PubMed] [PMC]
Hannan JP. The Structure-Function Relationships of Complement Receptor Type 2 (CR2; CD21).Curr Protein Pept Sci. 2016;17:463–87. [DOI] [PubMed]
Kimura H, Ito Y, Suzuki R, Nishiyama Y. Measuring Epstein–Barr virus (EBV) load: the significance and application for each EBV-associated disease.Rev Med Virol. 2008;18:305–19. [DOI] [PubMed]
Chesnokova LS, Nishimura SL, Hutt-Fletcher LM. Fusion of epithelial cells by Epstein–Barr virus proteins is triggered by binding of viral glycoproteins gHgL to integrins αvβ6 or αvβ8.Proc Natl Acad Sci U S A. 2009;106:20464–9. [DOI] [PubMed] [PMC]
Urquiza M, Melo-Cardenas J, Guevara T, Echeverria I, Rodriguez IC, Vanegas M, et al. α-Helix peptides designed from EBV-gH protein display higher antigenicity and induction of monocyte apoptosis than the native peptide.Amino Acids. 2010;39:1507–19. [DOI] [PubMed] [PMC]
Liu L, Sun H, Jiang Y, Hong J, Zheng Q, Li S, et al. Cryo-EM structure of EBV gHgL-gp42 in complex with mAb 6H2 (localized refinement) [Internet].wwPDB [cited 2025 Jan 30]. Available from: https://doi.org/10.2210/pdb7yp2/pdb
Sashihara J, Burbelo PD, Savoldo B, Pierson TC, Cohen JI. Human antibody titers to Epstein–Barr Virus (EBV) gp350 correlate with neutralization of infectivity better than antibody titers to EBV gp42 using a rapid flow cytometry-based EBV neutralization assay.Virology. 2009;391:249–56. [DOI] [PubMed] [PMC]
Cui X, Snapper CM. Epstein Barr Virus: Development of Vaccines and Immune Cell Therapy for EBV-Associated Diseases.Front Immunol. 2021;12:734471. [DOI] [PubMed] [PMC]
Bu W, Joyce MG, Nguyen H, Banh DV, Aguilar F, Tariq Z, et al. Immunization with Components of the Viral Fusion Apparatus Elicits Antibodies That Neutralize Epstein-Barr Virus in B Cells and Epithelial Cells.Immunity. 2019;50:1305–16.e6. [DOI] [PubMed] [PMC]
Cai J, Zhang B, Li Y, Zhu W, Akihisa T, Li W, et al. Prophylactic and Therapeutic EBV Vaccines: Major Scientific Obstacles, Historical Progress, and Future Direction.Vaccines (Basel). 2021;9:1290. [DOI] [PubMed] [PMC]
Snijder J, Ortego MS, Weidle C, Stuart AB, Gray MD, McElrath MJ, et al. An Antibody Targeting the Fusion Machinery Neutralizes Dual-Tropic Infection and Defines a Site of Vulnerability on Epstein-Barr Virus.Immunity. 2018;48:799–811.e9. [DOI] [PubMed] [PMC]
Cui X, Snapper CM. Development of novel vaccines against human cytomegalovirus.Hum Vaccin Immunother. 2019;15:2673–83. [DOI] [PubMed] [PMC]
Liu C, Li S, Qiao M, Zeng C, Liu X, Tang Y. GB and gH/gL fusion machinery: a promising target for vaccines to prevent Epstein-Barr virus infection.Arch Virol. 2024;169:167. [DOI] [PubMed]
Sun C, Fang XY, Bu GL, Zhong LY, Xie C, Zhao GX, et al. Structural basis of Epstein-Barr virus gp350 receptor recognition and neutralization.Cell Rep. 2025;44:115168. [DOI] [PubMed]
Urquiza M, Lopez R, Patiño H, Rosas JE, Patarroyo ME. Identification of three gp350/220 regions involved in Epstein-Barr virus invasion of host cells.J Biol Chem. 2005;280:35598–605. [DOI] [PubMed]
Tanner JE, Coinçon M, Leblond V, Hu J, Fang JM, Sygusch J, et al. Peptides designed to spatially depict the Epstein-Barr virus major virion glycoprotein gp350 neutralization epitope elicit antibodies that block virus-neutralizing antibody 72A1 interaction with the native gp350 molecule.J Virol. 2015;89:4932–41. [DOI] [PubMed] [PMC]
Chen WH, Bu W, Cohen JI, Kanekiyo M, Joyce MG. Crystal structure of human complement receptor 2 (CD21) in complex with Epstein-Barr virus major glycoprotein gp350 [Internet].wwPDB [cited 2025 Jan 30]. Available from: https://doi.org/10.2210/pdb8sm0/pdb
Urquiza M, Guevara T, Rodriguez C, Melo-Cardenas J, Vanegas M, Patarroyo ME. Decreasing the configurational entropy and the hydrophobicity of EBV-derived peptide 11389 increased its antigenicity, immunogenicity and its ability of inducing IL-6.Amino Acids. 2012;42:2165–75. [DOI] [PubMed]
Bingöl EN, Taştekil I, Yay C, Keskin N, Ozbek P. How Epstein-Barr virus envelope glycoprotein gp350 tricks the CR2? A molecular dynamics study.J Mol Graph Model. 2022;114:108196. [DOI] [PubMed]
Tanner JE, Hu J, Alfieri C. Construction and Characterization of a Humanized Anti-Epstein-Barr Virus gp350 Antibody with Neutralizing Activity in Cell Culture.Cancers (Basel). 2018;10:112. [DOI] [PubMed] [PMC]
Mutsvunguma LZ, Barasa A, Warden C, Foley J, Muniraju M, Mulama DH, et al. Identification of a Novel Neutralizing and Two Non-Neutralizing Epitopes on Epstein-Barr Virus gp350 Protein.BioRxiv 302844 [Preprint]. 2018 [cited 2025 Jan 30]. Available from: https://www.biorxiv.org/content/10.1101/302844v1
Alfieri C, inventor; Valorisation-HSJ, assignee. Antigenic epitopes from EBV gp350/220 and uses thereof.United States patent US 10016494. 2018 Jul 10.
Widodo, Pristiwanto B, Rifa’i M, Mustafa I, Huyop FZ. A single epitope of Epstein-Barr Virus stimulate IgG production in mice.Ann Med Surg (Lond). 2018;35:55–8. [DOI] [PubMed] [PMC]
Mutsvunguma LZ, Rodriguez E, Escalante GM, Muniraju M, Williams JC, Warden C, et al. Identification of multiple potent neutralizing and non-neutralizing antibodies against Epstein-Barr virus gp350 protein with potential for clinical application and as reagents for mapping immunodominant epitopes.Virology. 2019;536:1–15. [DOI] [PubMed] [PMC]
Alonso-Padilla J, Lafuente EM, Reche PA. Computer-Aided Design of an Epitope-Based Vaccine against Epstein-Barr Virus.J Immunol Res. 2017;2017:9363750. [DOI] [PubMed] [PMC]
Zheng J, Zeng X, Zeng L, Xu Y, Zhong Z, Wu Y, et al. Preparation of monoclonal antibodies against Epstein-Barr virus glycoprotein 350.Virus Genes. 2023;59:670–7. [DOI] [PubMed]
Ogembo JG, Muraswki MR, McGinnes LW, Parcharidou A, Sutiwisesak R, Tison T, et al. A chimeric EBV gp350/220-based VLP replicates the virion B-cell attachment mechanism and elicits long-lasting neutralizing antibodies in mice.J Transl Med. 2015;13:50. [DOI] [PubMed] [PMC]
Kanekiyo M, Bu W, Joyce MG, Meng G, Whittle JR, Baxa U, et al. Rational Design of an Epstein-Barr Virus Vaccine Targeting the Receptor-Binding Site.Cell. 2015;162:1090–100. [DOI] [PubMed] [PMC]
Zhang X, Zhao B, Ding M, Song S, Kang Y, Yu Y, et al. A novel vaccine candidate based on chimeric virus-like particle displaying multiple conserved epitope peptides induced neutralizing antibodies against EBV infection.Theranostics. 2020;10:5704–18. [DOI] [PubMed] [PMC]
Rühl J, Leung CS, Münz C. Vaccination against the Epstein–Barr virus.Cell Mol Life Sci. 2020;77:4315–24. [DOI] [PubMed] [PMC]
Dasari V, Sinha D, Neller MA, Smith C, Khanna R. Prophylactic and therapeutic strategies for Epstein-Barr virus-associated diseases: emerging strategies for clinical development.Expert Rev Vaccines. 2019;18:457–74. [DOI] [PubMed]
Yiu SPT, Dorothea M, Hui KF, Chiang AKS. Lytic Induction Therapy against Epstein-Barr Virus-Associated Malignancies: Past, Present, and Future.Cancers (Basel). 2020;12:2142. [DOI] [PubMed] [PMC]
López R, Urquiza M, Patino H, Suárez J, Reyes C, Patarroyo MA, et al. A B-lymphocyte binding peptide from BNRF1 induced antibodies inhibiting EBV-invasion of B-lymphocytes.Biochimie. 2005;87:985–92. [DOI] [PubMed]
Hayman IR, Temple RM, Burgess CK, Ferguson M, Liao J, Meyers C, et al. New insight into Epstein-Barr virus infection using models of stratified epithelium.PLoS Pathog. 2023;19:e1011040. [DOI] [PubMed] [PMC]
Rani A, Jakhmola S, Karnati S, Parmar HS, Chandra Jha H. Potential entry receptors for human γ-herpesvirus into epithelial cells: A plausible therapeutic target for viral infections.Tumour Virus Res. 2021;12:200227. [DOI] [PubMed] [PMC]
Kirschner AN, Omerovic J, Popov B, Longnecker R, Jardetzky TS. Soluble Epstein-Barr virus glycoproteins gH, gL, and gp42 form a 1:1:1 stable complex that acts like soluble gp42 in B-cell fusion but not in epithelial cell fusion.J Virol. 2006;80:9444–54. [DOI] [PubMed] [PMC]
Möhl BS, Sathiyamoorthy K, Jardetzky TS, Longnecker R. The conserved disulfide bond within domain II of Epstein-Barr virus gH has divergent roles in membrane fusion with epithelial cells and B cells.J Virol. 2014;88:13570–9. [DOI] [PubMed] [PMC]
Sathiyamoorthy K, Hu YX, Möhl BS, Chen J, Longnecker R, Jardetzky TS. Structural basis for Epstein-Barr virus host cell tropism mediated by gp42 and gHgL entry glycoproteins.Nat Commun. 2016;7:13557. [DOI] [PubMed] [PMC]
Chen WH, Kim J, Bu W, Board NL, Tsybovsky Y, Wang Y, et al. Epstein-Barr virus gH/gL has multiple sites of vulnerability for virus neutralization and fusion inhibition.Immunity. 2022;55:2135–48.e6. [DOI] [PubMed] [PMC]
Jones G, Jindal A, Ghani U, Kotelnikov S, Egbert M, Hashemi N, et al. Elucidation of protein function using computational docking and hotspot analysis by ClusPro and FTMap.Acta Crystallogr D Struct Biol. 2022;78:690–7. [DOI] [PubMed] [PMC]
Desta IT, Porter KA, Xia B, Kozakov D, Vajda S. Performance and Its Limits in Rigid Body Protein-Protein Docking.Structure. 2020;28:1071–81.e3. [DOI] [PubMed] [PMC]
Vajda S, Yueh C, Beglov D, Bohnuud T, Mottarella SE, Xia B, et al. New additions to the ClusPro server motivated by CAPRI.Proteins. 2017;85:435–44. [DOI] [PubMed] [PMC]
Kozakov D, Hall DR, Xia B, Porter KA, Padhorny D, Yueh C, et al. The ClusPro web server for protein-protein docking.Nat Protoc. 2017;12:255–78. [DOI] [PubMed] [PMC]
Kozakov D, Beglov D, Bohnuud T, Mottarella SE, Xia B, Hall DR, et al. How good is automated protein docking?Proteins. 2013;81:2159–66. [DOI] [PubMed] [PMC]
Xia B, Vajda S, Kozakov D. Accounting for pairwise distance restraints in FFT-based protein-protein docking.Bioinformatics. 2016;32:3342–4. [DOI] [PubMed] [PMC]
Brakebusch C, Bouvard D, Stanchi F, Sakai T, Fässler R. Integrins in invasive growth.J Clin Invest. 2002;109:999–1006. [DOI] [PubMed] [PMC]
Mason JM, Arndt KM. Coiled coil domains: stability, specificity, and biological implications.Chembiochem. 2004;5:170–6. [DOI] [PubMed]
Lopper M, Compton T. Coiled-coil domains in glycoproteins B and H are involved in human cytomegalovirus membrane fusion.J Virol. 2004;78:8333–41. [DOI] [PubMed] [PMC]
Wu L, Borza CM, Hutt-Fletcher LM. Mutations of Epstein-Barr virus gH that are differentially able to support fusion with B cells or epithelial cells.J Virol. 2005;79:10923–30. [DOI] [PubMed] [PMC]
Omerović J, Lev L, Longnecker R. The amino terminus of Epstein-Barr virus glycoprotein gH is important for fusion with epithelial and B cells.J Virol. 2005;79:12408–15. [DOI] [PubMed] [PMC]
Wu L, Hutt-Fletcher LM. Point mutations in EBV gH that abrogate or differentially affect B cell and epithelial cell fusion.Virology. 2007;363:148–55. [DOI] [PubMed] [PMC]
Hong J, Zhong L, Liu L, Wu Q, Zhang W, Chen K, et al. Non-overlapping epitopes on the gHgL-gp42 complex for the rational design of a triple-antibody cocktail against EBV infection.Cell Rep Med. 2023;4:101296. [DOI] [PubMed] [PMC]
Bieling M, Tischer S, Kalinke U, Blasczyk R, Buus S, Maecker-Kolhoff B, et al. Personalized adoptive immunotherapy for patients with EBV-associated tumors and complications: Evaluation of novel naturally processed and presented EBV-derived T-cell epitopes.Oncotarget. 2017;9:4737–57. [DOI] [PubMed] [PMC]
Deng CM, Wang TM, He YQ, Zhang WL, Xue WQ, Li DH, et al. Peptidome-wide association analysis of Epstein-Barr virus identifies epitope repertoires associated with nasopharyngeal carcinoma.J Med Virol. 2023;95:e28860. [DOI] [PubMed]
Ahmed M, Lopez-Albaitero A, Pankov D, Santich BH, Liu H, Yan S, et al. TCR-mimic bispecific antibodies targeting LMP2A show potent activity against EBV malignancies.JCI Insight. 2018;3:e97805. [DOI] [PubMed] [PMC]
Chan CK, Aimagambetova G, Ukybassova T, Kongrtay K, Azizan A. Human Papillomavirus Infection and Cervical Cancer: Epidemiology, Screening, and Vaccination—Review of Current Perspectives.J Oncol. 2019;2019:3257939. [DOI] [PubMed] [PMC]
Okunade KS. Human papillomavirus and cervical cancer.J Obstet Gynaecol. 2020;40:602–8. [DOI] [PubMed] [PMC]
Buck CB, Day PM, Trus BL. The papillomavirus major capsid protein L1.Virology. 2013;445:169–74. [DOI] [PubMed] [PMC]
Hernández-Silva CD, Ramírez de Arellano A, Pereira-Suárez AL, Ramírez-López IG. HPV and Cervical Cancer: Molecular and Immunological Aspects, Epidemiology and Effect of Vaccination in Latin American Women.Viruses. 2024;16:327. [DOI] [PubMed] [PMC]
Cardone G, Moyer AL, Cheng N, Thompson CD, Dvoretzky I, Lowy DR, et al. Electron cryo-microscopy of Human Papillomavirus Type 16 capsid [Internet].wwPDB [cited 2025 Jan 30]. Available from: https://doi.org/10.2210/pdb3j6r/pdb
Mustopa AZ, Meilina L, Irawan S, Ekawati N, Fathurahman AT, Triratna L, et al. Construction, expression, and in vitro assembly of virus-like particles of L1 protein of human papillomavirus type 52 in Escherichia coli BL21 DE3.J Genet Eng Biotechnol. 2022;20:19. [DOI] [PubMed] [PMC]
Graham SV. The human papillomavirus replication cycle, and its links to cancer progression: a comprehensive review.Clin Sci (Lond). 2017;131:2201–21. [DOI] [PubMed]
Han F, Guo XY, Jiang MX, Xia NS, Gu Y, Li SW. Structural biology of the human papillomavirus.Structure. 2024;32:1877–92. [DOI] [PubMed]
Roden RB, Kirnbauer R, Jenson AB, Lowy DR, Schiller JT. Interaction of papillomaviruses with the cell surface.J Virol. 1994;68:7260–6. [DOI] [PubMed] [PMC]
Wang JCK, Baddock HT, Mafi A, Foe IT, Bratkowski M, Lin TY, et al. Structure of the p53 degradation complex from HPV16.Nat Commun. 2024;15:1842. [DOI] [PubMed] [PMC]
Li S, Hong X, Wei Z, Xie M, Li W, Liu G, et al. Ubiquitination of the HPV Oncoprotein E6 Is Critical for E6/E6AP-Mediated p53 Degradation.Front Microbiol. 2019;10:2483. [DOI] [PubMed] [PMC]
Fischer M, Uxa S, Stanko C, Magin TM, Engeland K. Human papilloma virus E7 oncoprotein abrogates the p53-p21-DREAM pathway.Sci Rep. 2017;7:2603. [DOI] [PubMed] [PMC]
Jansma AL, Martinez-Yamout MA, Liao R, Sun P, Dyson HJ, Wright PE. The high-risk HPV16 E7 oncoprotein mediates interaction between the transcriptional coactivator CBP and the retinoblastoma protein pRb.J Mol Biol. 2014;426:4030–48. [DOI] [PubMed] [PMC]
Mandigo AC, Tomlins SA, Kelly WK, Knudsen KE. Relevance of pRB Loss in Human Malignancies.Clin Cancer Res. 2022;28:255–64. [DOI] [PubMed] [PMC]
Temaj G, Chichiarelli S, Telkoparan-Akillilar P, Saha S, Nuhii N, Hadziselimovic R, et al. P53: A key player in diverse cellular processes including nuclear stress and ribosome biogenesis, highlighting potential therapeutic compounds.Biochem Pharmacol. 2024;226:116332. [DOI] [PubMed]
Li S, Sampson C, Liu C, Piao HL, Liu HX. Integrin signaling in cancer: bidirectional mechanisms and therapeutic opportunities.Cell Commun Signal. 2023;21:266. [DOI] [PubMed] [PMC]
Raff AB, Woodham AW, Raff LM, Skeate JG, Yan L, Da Silva DM, et al. The evolving field of human papillomavirus receptor research: a review of binding and entry.J Virol. 2013;87:6062–72. [DOI] [PubMed] [PMC]
Chen XS, Garcea RL, Goldberg I, Casini G, Harrison SC. Structure of small virus-like particles assembled from the L1 protein of human papillomavirus 16.Mol Cell. 2000;5:557–67. [DOI] [PubMed]
Vera-Bravo R, Ocampo M, Urquiza M, García JE, Rodríguez LE, Puentes A, et al. Human papillomavirus type 16 and 18 L1 protein peptide binding to VERO and HeLa cells inhibits their VLPs binding.Int J Cancer. 2003;107:416–24. [DOI] [PubMed]
Urquiza M, Guevara T, Espejo F, Bravo MM, Rivera Z, Patarroyo ME. Two L1-peptides are excellent tools for serological detection of HPV-associated cervical carcinoma lesions.Biochem Biophys Res Commun. 2005;332:224–32. [DOI] [PubMed]
Urquiza M, Sánchez R, Amaya J, León S, Acosta J, Patarroyo MA, et al. Specificity of L1 peptides versus virus-like particles for detection of human papillomavirus-positive cervical lesions in females attending Engativa Hospital, Bogota, Colombia.J Clin Microbiol. 2008;46:3714–20. [DOI] [PubMed] [PMC]
Urquiza M, Guevara T, Sanchez R, Vanegas M, Patarroyo ME. A non-variable L1-peptide displays high sensitivity and specificity for detecting women having human papillomavirus-associated cervical lesions.Peptides. 2008;29:957–62. [DOI] [PubMed]
Solares AM, Baladron I, Ramos T, Valenzuela C, Borbon Z, Fanjull S, et al. Safety and Immunogenicity of a Human Papillomavirus Peptide Vaccine (CIGB-228) in Women with High-Grade Cervical Intraepithelial Neoplasia: First-in-Human, Proof-of-Concept Trial.ISRN Obstet Gynecol. 2011;2011:292951. [DOI] [PubMed] [PMC]
Wang R, Pan W, Jin L, Huang W, Li Y, Wu D, et al. Human papillomavirus vaccine against cervical cancer: Opportunity and challenge.Cancer Lett. 2020;471:88–102. [DOI] [PubMed]
Sercarz EE, Maverakis E. Mhc-guided processing: binding of large antigen fragments.Nat Rev Immunol. 2003;3:621–9. [DOI] [PubMed]
Mo Y, Ma J, Zhang H, Shen J, Chen J, Hong J, et al. Prophylactic and Therapeutic HPV Vaccines: Current Scenario and Perspectives.Front Cell Infect Microbiol. 2022;12:909223. [DOI] [PubMed] [PMC]
Wang J, Wang Q, Ma L, Lv K, Han L, Chen Y, et al. Development of an mRNA-based therapeutic vaccine mHTV-03E2 for high-risk HPV-related malignancies.Mol Ther. 2024;32:2340–56. [DOI] [PubMed]
Kim DY, Park H, Cho S, Yoon HS. Effectiveness of New 5-Fluorouracil/Salicylic Acid Application Method for Periungual Warts: A Descriptive Study.Ann Dermatol. 2020;32:345–7. [DOI] [PubMed] [PMC]
Mlynarczyk-Bonikowska B, Rudnicka L. HPV Infections—Classification, Pathogenesis, and Potential New Therapies.Int J Mol Sci. 2024;25:7616. [DOI] [PubMed] [PMC]
Petruzziello A, Marigliano S, Loquercio G, Cozzolino A, Cacciapuoti C. Global epidemiology of hepatitis C virus infection: An up-date of the distribution and circulation of hepatitis C virus genotypes.World J Gastroenterol. 2016;22:7824–40. [DOI] [PubMed] [PMC]
Bernal LA, Soti V. Hepatitis C Virus: Insights Into Its History, Treatment, Challenges, and Future Directions.Cureus. 2023;15:e43924. [DOI] [PubMed] [PMC]
Zumaeta Villena E. Transmission routes of hepatitis C virus infection.Ann Hepatol. 2006;5:S12–4. [DOI]
Palacios A, Taylor L, Haue L, Luftig RB, Visoná KA. Development of low cost peptide-based anti-hepatitis C virus screening and confirmatory assays: comparison with commercially available tests.J Med Virol. 1999;58:221–6. [DOI] [PubMed]
Warncke SR, Knudsen CR. Detection methods targeting the positive- and negative-sense RNA transcripts from plus-stranded RNA viruses.APMIS. 2022;130:284–92. [DOI] [PubMed] [PMC]
Sallam M, Khalil R. Contemporary Insights into Hepatitis C Virus: A Comprehensive Review.Microorganisms. 2024;12:1035. [DOI] [PubMed] [PMC]
Kato N. Molecular virology of hepatitis C virus.Acta Med Okayama. 2001;55:133–59. [DOI] [PubMed]
Torrents de la Peña A, Sliepen K, Eshun-Wilson L, Newby ML, Allen JD, Zon I, et al. Structure of the hepatitis C virus E1E2 glycoprotein complex.Science. 2022;378:263–9. [DOI] [PubMed] [PMC]
Kumar A, Hossain RA, Yost SA, Bu W, Wang Y, Dearborn AD, et al. Structural insights into hepatitis C virus receptor binding and entry.Nature. 2021;598:521–5. [DOI] [PubMed] [PMC]
Harris HJ, Farquhar MJ, Mee CJ, Davis C, Reynolds GM, Jennings A, et al. CD81 and claudin 1 coreceptor association: role in hepatitis C virus entry.J Virol. 2008;82:5007–20. [DOI] [PubMed] [PMC]
Douam F, Lavillette D, Cosset FL. The mechanism of HCV entry into host cells.Prog Mol Biol Transl Sci. 2015;129:63–107. [DOI] [PubMed]
Colpitts CC, Tsai PL, Zeisel MB. Hepatitis C Virus Entry: An Intriguingly Complex and Highly Regulated Process.Int J Mol Sci. 2020;21:2091. [DOI] [PubMed] [PMC]
Bartosch B, Cosset FL. Cell entry of hepatitis C virus.Virology. 2006;348:1–12. [DOI] [PubMed]
Frumento N, Flyak AI, Bailey JR. Mechanisms of HCV resistance to broadly neutralizing antibodies.Curr Opin Virol. 2021;50:23–9. [DOI] [PubMed] [PMC]
Chigbu DI, Loonawat R, Sehgal M, Patel D, Jain P. Hepatitis C Virus Infection: Host–Virus Interaction and Mechanisms of Viral Persistence.Cells. 2019;8:376. [DOI] [PubMed] [PMC]
Garcia JE, Puentes A, Súarez J, López R, Vera R, Rodríguez LE, et al. Hepatitis C virus (HCV) E1 and E2 protein regions that specifically bind to HepG2 cells.J Hepatol. 2002;36:254–62. [DOI] [PubMed]
Meshram R, Kolte B, Gacche R. Reverse vaccinology approach for identification of epitopes from E1 protein as peptide vaccine against HCV: A proof of concept.Vaccine. 2024;42:126106. [DOI] [PubMed]
Ishida C, Matsumoto K, Fukada K, Matsushita K, Shiraki H, Maeda Y. Detection of antibodies to hepatitis C virus (HCV) structural proteins in anti-HCV-positive sera by an enzyme-linked immunosorbent assay using synthetic peptides as antigens.J Clin Microbiol. 1993;31:936–40. [DOI] [PubMed] [PMC]
Zhou YH, Shimizu YK, Esumi M. Monoclonal antibodies to the hypervariable region 1 of hepatitis C virus capture virus and inhibit virus adsorption to susceptible cells in vitro.Virology. 2000;269:276–83. [DOI] [PubMed]
Zibert A, Dudziak P, Schreier E, Roggendorf M. Characterization of antibody response to hepatitis C virus protein E2 and significance of hypervariable region 1-specific antibodies in viral neutralization.Arch Virol. 1997;142:523–34. [DOI] [PubMed]
Shimizu YK, Igarashi H, Kiyohara T, Cabezon T, Farci P, Purcell RH, et al. A hyperimmune serum against a synthetic peptide corresponding to the hypervariable region 1 of hepatitis C virus can prevent viral infection in cell cultures.Virology. 1996;223:409–12. [DOI] [PubMed]
Esumi M, Rikihisa T, Nishimura S, Goto J, Mizuno K, Zhou YH, et al. Experimental vaccine activities of recombinant E1 and E2 glycoproteins and hypervariable region 1 peptides of hepatitis C virus in chimpanzees.Arch Virol. 1999;144:973–80. [DOI] [PubMed]
Choo QL, Kuo G, Ralston R, Weiner A, Chien D, Van Nest G, et al. Vaccination of chimpanzees against infection by the hepatitis C virus.Proc Natl Acad Sci U S A. 1994;91:1294–8. [DOI] [PubMed] [PMC]
Farci P, Shimoda A, Wong D, Cabezon T, De Gioannis D, Strazzera A, et al. Prevention of hepatitis C virus infection in chimpanzees by hyperimmune serum against the hypervariable region 1 of the envelope 2 protein.Proc Natl Acad Sci U S A. 1996;93:15394–9. [DOI] [PubMed] [PMC]
Sekiya H, Kato N, Ootsuyama Y, Nakazawa T, Yamauchi K, Shimotohno K. Genetic alterations of the putative envelope proteins encoding region of the hepatitis C virus in the progression to relapsed phase from acute hepatitis: humoral immune response to hypervariable region 1.Int J Cancer. 1994;57:664–70. [DOI] [PubMed]
Kato N, Ootsuyama Y, Sekiya H, Ohkoshi S, Nakazawa T, Hijikata M, et al. Genetic drift in hypervariable region 1 of the viral genome in persistent hepatitis C virus infection.J Virol. 1994;68:4776–84. [DOI] [PubMed] [PMC]
Mink MA, Benichou S, Madaule P, Tiollais P, Prince AM, Inchauspe G. Characterization and Mapping of a B-Cell Immunogenic Domain in Hepatitis C Virus E2 Glycoprotein Using a Yeast Peptide Library.Virology. 1994;200:246–55. [DOI] [PubMed]
Lee JW, Kim Km, Jung SH, Lee KJ, Choi EC, Sung YC, et al. Identification of a domain containing B-cell epitopes in hepatitis C virus E2 glycoprotein by using mouse monoclonal antibodies.J Virol. 1999;73:11–8. [DOI] [PubMed] [PMC]
Sorbo MC, Cento V, Di Maio VC, Howe AYM, Garcia F, Perno CF, et al. Hepatitis C virus drug resistance associated substitutions and their clinical relevance: Update 2018.Drug Resist Updat. 2018;37:17–39. [DOI] [PubMed]
Yin P, Zhang L, Ye F, Deng Y, Lu S, Li YP, et al. A screen for inhibitory peptides of hepatitis C virus identifies a novel entry inhibitor targeting E1 and E2.Sci Rep. 2017;7:3976. [DOI] [PubMed] [PMC]
Liu R, Tewari M, Kong R, Zhang R, Ingravallo P, Ralston R. A peptide derived from hepatitis C virus E2 envelope protein inhibits a post-binding step in HCV entry.Antiviral Res. 2010;86:172–9. [DOI] [PubMed]
Augestad EH, Bukh J, Prentoe J. Hepatitis C virus envelope protein dynamics and the link to hypervariable region 1.Curr Opin Virol. 2021;50:69–75. [DOI] [PubMed]
