{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,18]],"date-time":"2026-06-18T16:49:14Z","timestamp":1781801354332,"version":"3.54.5"},"reference-count":66,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2025,4,3]],"date-time":"2025-04-03T00:00:00Z","timestamp":1743638400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"},{"start":{"date-parts":[[2025,4,3]],"date-time":"2025-04-03T00:00:00Z","timestamp":1743638400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"}],"funder":[{"DOI":"10.13039\/501100005357","name":"Agent\u00fara na Podporu V\u00fdskumu a V\u00fdvoja","doi-asserted-by":"publisher","award":["APVV-22-0084"],"award-info":[{"award-number":["APVV-22-0084"]}],"id":[{"id":"10.13039\/501100005357","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100005357","name":"Agent\u00fara na Podporu V\u00fdskumu a V\u00fdvoja","doi-asserted-by":"publisher","award":["APVV-23-0348"],"award-info":[{"award-number":["APVV-23-0348"]}],"id":[{"id":"10.13039\/501100005357","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100006109","name":"Vedeck\u00e1 Grantov\u00e1 Agent\u00fara M\u0160VVa\u0160 SR a SAV","doi-asserted-by":"publisher","award":["VEGA1\/0381\/23"],"award-info":[{"award-number":["VEGA1\/0381\/23"]}],"id":[{"id":"10.13039\/501100006109","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100006109","name":"Vedeck\u00e1 Grantov\u00e1 Agent\u00fara M\u0160VVa\u0160 SR a SAV","doi-asserted-by":"publisher","award":["VEGA1\/0348\/22"],"award-info":[{"award-number":["VEGA1\/0348\/22"]}],"id":[{"id":"10.13039\/501100006109","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100018225","name":"EuroNanoMed III","doi-asserted-by":"publisher","award":["EURONANOMED2021-105"],"award-info":[{"award-number":["EURONANOMED2021-105"]}],"id":[{"id":"10.13039\/100018225","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Sci Rep"],"DOI":"10.1038\/s41598-025-95449-1","type":"journal-article","created":{"date-parts":[[2025,4,4]],"date-time":"2025-04-04T21:41:51Z","timestamp":1743802911000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Peptides developed against receptor binding sites of the E glycoprotein neutralize tick-borne encephalitis virus"],"prefix":"10.1038","volume":"15","author":[{"given":"Patr\u00edcia","family":"Petrou\u0161kov\u00e1","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katar\u00edna","family":"Bhide","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Evel\u00edna","family":"Mochn\u00e1\u010dov\u00e1","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Amod","family":"Kulkarni","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jana","family":"Jozefiakov\u00e1","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zuzana","family":"Tk\u00e1\u010dov\u00e1","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tom\u00e1\u0161","family":"Ma\u013earik","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katar\u00edna","family":"Kuckov\u00e1","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lea","family":"Talpa\u0161ov\u00e1","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jakub","family":"V\u00edglask\u00fd","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"\u00c1d\u00e1m","family":"Kev\u00e9ly","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kamila","family":"Ko\u010di","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eva","family":"Nov\u00e1kov\u00e1","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5560-806X","authenticated-orcid":false,"given":"Juraj","family":"Ko\u010di","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mangesh","family":"Bhide","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2025,4,3]]},"reference":[{"key":"95449_CR1","doi-asserted-by":"publisher","first-page":"129","DOI":"10.1016\/S0166-3542(02)00206-1","volume":"57","author":"TS Gritsun","year":"2003","unstructured":"Gritsun, T. S., Lashkevich, V. A. & Gould, E. A. Tick-borne encephalitis. Antiviral Res. 57, 129\u2013146 (2003).","journal-title":"Antiviral Res."},{"key":"95449_CR2","doi-asserted-by":"crossref","unstructured":"Beaute, J., Spiteri, G., Warns-Petit, E. & Zeller, H. Tick-borne encephalitis in Europe, 2012 to 2016. Euro Surveillance 23 (2018).","DOI":"10.2807\/1560-7917.ES.2018.23.45.1800201"},{"key":"95449_CR3","doi-asserted-by":"publisher","first-page":"221","DOI":"10.1016\/j.vetmic.2009.08.024","volume":"140","author":"G Dobler","year":"2010","unstructured":"Dobler, G. Zoonotic tick-borne flaviviruses. Vet. Microbiol. 140, 221\u2013228 (2010).","journal-title":"Vet. Microbiol."},{"key":"95449_CR4","doi-asserted-by":"publisher","first-page":"48","DOI":"10.1038\/s41392-022-00904-4","volume":"7","author":"L Wang","year":"2022","unstructured":"Wang, L. et al. Therapeutic peptides: Current applications and future directions. Signal. Transduct. Target. Ther. 7, 48 (2022).","journal-title":"Signal. Transduct. Target. Ther."},{"key":"95449_CR5","doi-asserted-by":"publisher","first-page":"170402","DOI":"10.1016\/j.peptides.2020.170402","volume":"134","author":"S Al-Azzam","year":"2020","unstructured":"Al-Azzam, S. et al. Peptides to combat viral infectious diseases. Peptides 134, 170402 (2020).","journal-title":"Peptides"},{"key":"95449_CR6","doi-asserted-by":"crossref","unstructured":"Lee, Y. J., Shirkey, J. D., Park, J., Bisht, K. & Cowan, A. J. An overview of antiviral peptides and rational biodesign considerations. Biodes. Res. 2022, 9898241 (2022).","DOI":"10.34133\/2022\/9898241"},{"key":"95449_CR7","doi-asserted-by":"crossref","unstructured":"Mazzon, M. & Marsh, M. Targeting viral entry as a strategy for broad-spectrum antivirals. F1000Res 8 (2019).","DOI":"10.12688\/f1000research.19694.1"},{"key":"95449_CR8","doi-asserted-by":"publisher","first-page":"398","DOI":"10.3389\/fcimb.2018.00398","volume":"8","author":"MK Zakaria","year":"2018","unstructured":"Zakaria, M. K., Carletti, T. & Marcello, A. Cellular targets for the treatment of flavivirus infections. Front. Cell. Infect. Microbiol. 8, 398 (2018).","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"95449_CR9","doi-asserted-by":"publisher","first-page":"8","DOI":"10.1186\/s12929-016-0223-x","volume":"23","author":"CH Wu","year":"2016","unstructured":"Wu, C. H., Liu, I. J., Lu, R. M. & Wu, H. C. Advancement and applications of peptide phage display technology in biomedical science. J. Biomed. Sci. 23, 8 (2016).","journal-title":"J. Biomed. Sci."},{"key":"95449_CR10","doi-asserted-by":"publisher","first-page":"3499","DOI":"10.3390\/molecules16053499","volume":"16","author":"G Castel","year":"2011","unstructured":"Castel, G., Chteoui, M., Heyd, B. & Tordo, N. Phage display of combinatorial peptide libraries: Application to antiviral research. Molecules 16, 3499\u20133518 (2011).","journal-title":"Molecules"},{"key":"95449_CR11","doi-asserted-by":"publisher","first-page":"2047","DOI":"10.1128\/JVI.01840-06","volume":"81","author":"F Bai","year":"2007","unstructured":"Bai, F. et al. Antiviral peptides targeting the West nile virus envelope protein. J. Virol. 81, 2047\u20132055 (2007).","journal-title":"J. Virol."},{"key":"95449_CR12","doi-asserted-by":"publisher","first-page":"1237","DOI":"10.1292\/jvms.67.1237","volume":"67","author":"M Ozawa","year":"2005","unstructured":"Ozawa, M., Ohashi, K. & Onuma, M. Identification and characterization of peptides binding to Newcastle disease virus by phage display. J. Vet. Med. Sci. 67, 1237\u20131241 (2005).","journal-title":"J. Vet. Med. Sci."},{"key":"95449_CR13","doi-asserted-by":"publisher","first-page":"981","DOI":"10.1007\/s00705-001-0778-y","volume":"147","author":"P Ramanujam","year":"2002","unstructured":"Ramanujam, P., Tan, W. S., Nathan, S. & Yusoff, K. Novel peptides that inhibit the propagation of Newcastle disease virus. Arch. Virol. 147, 981\u2013993 (2002).","journal-title":"Arch. Virol."},{"key":"95449_CR14","doi-asserted-by":"publisher","first-page":"4244","DOI":"10.1128\/JVI.01270-06","volume":"81","author":"Q Deng","year":"2007","unstructured":"Deng, Q. et al. Identification and characterization of peptides that interact with hepatitis B virus via the putative receptor binding site. J. Virol. 81, 4244\u20134254 (2007).","journal-title":"J. Virol."},{"key":"95449_CR15","doi-asserted-by":"crossref","unstructured":"de la Guardia, C., Quijada, M. & Lleonart, R. Phage-displayed peptides selected to bind envelope glycoprotein show antiviral activity against dengue virus serotype 2. Adv. Virol. 2017, 1827341 (2017).","DOI":"10.1155\/2017\/1827341"},{"key":"95449_CR16","doi-asserted-by":"publisher","first-page":"110","DOI":"10.1016\/j.virol.2017.04.012","volume":"507","author":"M Palus","year":"2017","unstructured":"Palus, M. et al. Tick-borne encephalitis virus infects human brain microvascular endothelial cells without compromising blood-brain barrier integrity. Virology 507, 110\u2013122 (2017).","journal-title":"Virology"},{"key":"95449_CR17","doi-asserted-by":"publisher","first-page":"e20472","DOI":"10.1371\/journal.pone.0020472","volume":"6","author":"D Ruzek","year":"2011","unstructured":"Ruzek, D., Salat, J., Singh, S. K. & Kopecky, J. Breakdown of the blood-brain barrier during tick-borne encephalitis in mice is not dependent on CD8+ T-cells. PLoS One 6, e20472 (2011).","journal-title":"PLoS One"},{"key":"95449_CR18","doi-asserted-by":"publisher","first-page":"8765","DOI":"10.1128\/jvi.70.12.8765-8772.1996","volume":"70","author":"Y Chen","year":"1996","unstructured":"Chen, Y., Maguire, T. & Marks, R. M. Demonstration of binding of dengue virus envelope protein to target cells. J. Virol. 70, 8765\u20138772 (1996).","journal-title":"J. Virol."},{"key":"95449_CR19","doi-asserted-by":"publisher","first-page":"284","DOI":"10.1186\/s12974-020-01943-w","volume":"17","author":"R Lindqvist","year":"2020","unstructured":"Lindqvist, R. et al. The envelope protein of tick-borne encephalitis virus influences neuron entry, pathogenicity, and vaccine protection. J. Neuroinflamm. 17, 284 (2020).","journal-title":"J. Neuroinflamm."},{"key":"95449_CR20","doi-asserted-by":"publisher","first-page":"291","DOI":"10.1038\/375291a0","volume":"375","author":"FA Rey","year":"1995","unstructured":"Rey, F. A., Heinz, F. X., Mandl, C., Kunz, C. & Harrison, S. C. The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution. Nature 375, 291\u2013298 (1995).","journal-title":"Nature"},{"key":"95449_CR21","doi-asserted-by":"publisher","first-page":"564","DOI":"10.1128\/jvi.63.2.564-571.1989","volume":"63","author":"CW Mandl","year":"1989","unstructured":"Mandl, C. W., Guirakhoo, F., Holzmann, H., Heinz, F. X. & Kunz, C. Antigenic structure of the flavivirus envelope protein E at the molecular level, using tick-borne encephalitis virus as a model. J. Virol. 63, 564\u2013571 (1989).","journal-title":"J. Virol."},{"key":"95449_CR22","doi-asserted-by":"publisher","first-page":"378","DOI":"10.1128\/JVI.78.1.378-388.2004","volume":"78","author":"JJ Hung","year":"2004","unstructured":"Hung, J. J. et al. An external loop region of domain III of dengue virus type 2 envelope protein is involved in serotype-specific binding to mosquito but not mammalian cells. J. Virol. 78, 378\u2013388 (2004).","journal-title":"J. Virol."},{"key":"95449_CR23","doi-asserted-by":"publisher","first-page":"179","DOI":"10.1016\/j.antiviral.2012.03.002","volume":"94","author":"C Li","year":"2012","unstructured":"Li, C. et al. Inhibition of Japanese encephalitis virus entry into the cells by the envelope glycoprotein domain III (EDIII) and the loop3 peptide derived from EDIII. Antiviral Res. 94, 179\u2013183 (2012).","journal-title":"Antiviral Res."},{"key":"95449_CR24","doi-asserted-by":"publisher","first-page":"405","DOI":"10.1099\/vir.0.80411-0","volume":"86","author":"JJH Chu","year":"2005","unstructured":"Chu, J. J. H. et al. Inhibition of West nile virus entry by using a recombinant domain III from the envelope glycoprotein. J. Gen. Virol. 86, 405\u2013412 (2005).","journal-title":"J. Gen. Virol."},{"key":"95449_CR25","doi-asserted-by":"publisher","first-page":"114","DOI":"10.1016\/j.virol.2013.03.011","volume":"441","author":"JT Roehrig","year":"2013","unstructured":"Roehrig, J. T. et al. Mutation of the dengue virus type 2 envelope protein heparan sulfate binding sites or the domain III lateral ridge blocks replication in vero cells prior to membrane fusion. Virology 441, 114\u2013125 (2013).","journal-title":"Virology"},{"key":"95449_CR26","doi-asserted-by":"publisher","first-page":"7769","DOI":"10.1128\/JVI.75.16.7769-7773.2001","volume":"75","author":"WD Crill","year":"2001","unstructured":"Crill, W. D. & Roehrig, J. T. Monoclonal antibodies that bind to domain III of dengue virus E glycoprotein are the most efficient blockers of virus adsorption to vero cells. J. Virol. 75, 7769\u20137773 (2001).","journal-title":"J. Virol."},{"key":"95449_CR27","doi-asserted-by":"publisher","first-page":"1163","DOI":"10.1038\/s41598-020-58305-y","volume":"10","author":"P Mertinkova","year":"2020","unstructured":"Mertinkova, P. et al. A simple and rapid pipeline for identification of receptor-binding sites on the surface proteins of pathogens. Sci. Rep. 10, 1163 (2020).","journal-title":"Sci. Rep."},{"key":"95449_CR28","doi-asserted-by":"publisher","first-page":"8863","DOI":"10.1038\/s41598-022-13043-1","volume":"12","author":"K Bhide","year":"2022","unstructured":"Bhide, K. et al. Signaling events evoked by domain III of envelop glycoprotein of tick-borne encephalitis virus and West nile virus in human brain microvascular endothelial cells. Sci. Rep. 12, 8863 (2022).","journal-title":"Sci. Rep."},{"key":"95449_CR29","doi-asserted-by":"publisher","first-page":"9601","DOI":"10.1128\/JVI.74.20.9601-9609.2000","volume":"74","author":"CW Mandl","year":"2000","unstructured":"Mandl, C. W., Allison, S. L., Holzmann, H., Meixner, T. & Heinz, F. X. Attenuation of tick-borne encephalitis virus by structure-based site-specific mutagenesis of a putative flavivirus receptor binding site. J. Virol. 74, 9601\u20139609 (2000).","journal-title":"J. Virol."},{"key":"95449_CR30","doi-asserted-by":"publisher","first-page":"5668","DOI":"10.1128\/JVI.00293-15","volume":"89","author":"H Liu","year":"2015","unstructured":"Liu, H. et al. Structure-based mutational analysis of several sites in the E protein: Implications for understanding the entry mechanism of Japanese encephalitis virus. J. Virol. 89, 5668\u20135686 (2015).","journal-title":"J. Virol."},{"issue":"Pt 1","key":"95449_CR31","doi-asserted-by":"publisher","first-page":"31","DOI":"10.1099\/0022-1317-78-1-31","volume":"78","author":"H Holzmann","year":"1997","unstructured":"Holzmann, H., Stiasny, K., Ecker, M., Kunz, C. & Heinz, F. X. Characterization of monoclonal antibody-escape mutants of tick-borne encephalitis virus with reduced neuroinvasiveness in mice. J. Gen. Virol. 78 (Pt 1), 31\u201337 (1997).","journal-title":"J. Gen. Virol."},{"key":"95449_CR32","doi-asserted-by":"publisher","first-page":"5156","DOI":"10.1128\/jvi.64.10.5156-5159.1990","volume":"64","author":"H Holzmann","year":"1990","unstructured":"Holzmann, H., Heinz, F. X., Mandl, C. W., Guirakhoo, F. & Kunz, C. A single amino acid substitution in envelope protein E of tick-borne encephalitis virus leads to attenuation in the mouse model. J. Virol. 64, 5156\u20135159 (1990).","journal-title":"J. Virol."},{"key":"95449_CR33","doi-asserted-by":"publisher","first-page":"8867","DOI":"10.1128\/JVI.74.19.8867-8875.2000","volume":"74","author":"E Lee","year":"2000","unstructured":"Lee, E. & Lobigs, M. Substitutions at the putative receptor-binding site of an encephalitic flavivirus alter virulence and host cell tropism and reveal a role for glycosaminoglycans in entry. J. Virol. 74, 8867\u20138875 (2000).","journal-title":"J. Virol."},{"key":"95449_CR34","doi-asserted-by":"publisher","first-page":"5627","DOI":"10.1128\/JVI.75.12.5627-5637.2001","volume":"75","author":"CW Mandl","year":"2001","unstructured":"Mandl, C. W. et al. Adaptation of tick-borne encephalitis virus to BHK-21 cells results in the formation of multiple Heparan sulfate binding sites in the envelope protein and attenuation in vivo. J. Virol. 75, 5627\u20135637 (2001).","journal-title":"J. Virol."},{"key":"95449_CR35","doi-asserted-by":"publisher","first-page":"104673","DOI":"10.1016\/j.antiviral.2019.104673","volume":"174","author":"J Wei","year":"2020","unstructured":"Wei, J. et al. Antiviral activity of phage display-selected peptides against Japanese encephalitis virus infection in vitro and in vivo. Antiviral Res. 174, 104673 (2020).","journal-title":"Antiviral Res."},{"key":"95449_CR36","doi-asserted-by":"publisher","first-page":"7","DOI":"10.1016\/j.antiviral.2014.01.011","volume":"104","author":"X Zu","year":"2014","unstructured":"Zu, X. et al. Peptide inhibitor of Japanese encephalitis virus infection targeting envelope protein domain III. Antiviral Res. 104, 7\u201314 (2014).","journal-title":"Antiviral Res."},{"key":"95449_CR37","doi-asserted-by":"publisher","first-page":"20131","DOI":"10.1038\/s41598-021-99696-w","volume":"11","author":"P Mertinkova","year":"2021","unstructured":"Mertinkova, P. et al. Development of peptides targeting receptor binding site of the envelope glycoprotein to contain the West nile virus infection. Sci. Rep. 11, 20131 (2021).","journal-title":"Sci. Rep."},{"key":"95449_CR38","first-page":"3733","volume":"57","author":"YS Gho","year":"1997","unstructured":"Gho, Y. S., Lee, J. E., Oh, K. S., Bae, D. G. & Chae, C. B. Development of antiangiogenin peptide using a phage-displayed peptide library. Cancer Res. 57, 3733\u20133740 (1997).","journal-title":"Cancer Res."},{"key":"95449_CR39","doi-asserted-by":"publisher","first-page":"509","DOI":"10.1002\/prot.340140411","volume":"14","author":"KT O\u2019Neil","year":"1992","unstructured":"O\u2019Neil, K. T. et al. Identification of novel peptide antagonists for GPIIb\/IIIa from a conformationally constrained phage peptide library. Proteins 14, 509\u2013515 (1992).","journal-title":"Proteins"},{"key":"95449_CR40","doi-asserted-by":"publisher","first-page":"27","DOI":"10.1002\/jmv.10266","volume":"69","author":"KL Ho","year":"2003","unstructured":"Ho, K. L., Yusoff, K., Seow, H. F. & Tan, W. S. Selection of high affinity ligands to hepatitis B core antigen from a phage-displayed cyclic peptide library. J. Med. Virol. 69, 27\u201332 (2003).","journal-title":"J. Med. Virol."},{"key":"95449_CR41","doi-asserted-by":"publisher","first-page":"35","DOI":"10.1016\/j.jcv.2005.01.007","volume":"34","author":"WS Tan","year":"2005","unstructured":"Tan, W. S., Tan, G. H., Yusoff, K. & Seow, H. F. A phage-displayed cyclic peptide that interacts tightly with the immunodominant region of hepatitis B surface antigen. J. Clin. Virol. 34, 35\u201341 (2005).","journal-title":"J. Clin. Virol."},{"key":"95449_CR42","first-page":"682","volume":"20","author":"HB Luo","year":"2004","unstructured":"Luo, H. B., Zheng, S. G., Zhu, P. & Fu, N. Study on mimotopes of E. coli lipopolysaccharide 2630. J. Cell. Mol. Immunol. 20, 682\u2013685 (2004).","journal-title":"J. Cell. Mol. Immunol."},{"key":"95449_CR43","doi-asserted-by":"publisher","first-page":"401","DOI":"10.1146\/annurev.biophys.26.1.401","volume":"26","author":"HB Lowman","year":"1997","unstructured":"Lowman, H. B. Bacteriophage display and discovery of peptide leads for drug development. Annu. Rev. Biophys. Biomol. Struct. 26, 401\u2013424 (1997).","journal-title":"Annu. Rev. Biophys. Biomol. Struct."},{"key":"95449_CR44","doi-asserted-by":"publisher","first-page":"4306","DOI":"10.1021\/jm701600a","volume":"51","author":"BE Haug","year":"2008","unstructured":"Haug, B. E., Stensen, W., Kalaaji, M., Rekdal, O. & Svendsen, J. S. Synthetic antimicrobial peptidomimetics with therapeutic potential. J. Med. Chem. 51, 4306\u20134314 (2008).","journal-title":"J. Med. Chem."},{"key":"95449_CR45","doi-asserted-by":"publisher","first-page":"1687","DOI":"10.1016\/j.bbamem.2008.09.013","volume":"1788","author":"K Matsuzaki","year":"2009","unstructured":"Matsuzaki, K. Control of cell selectivity of antimicrobial peptides. Biochim. Biophys. Acta 1788, 1687\u20131692 (2009).","journal-title":"Biochim. Biophys. Acta"},{"key":"95449_CR46","doi-asserted-by":"publisher","first-page":"1173","DOI":"10.1002\/jps.20627","volume":"95","author":"K Amin","year":"2006","unstructured":"Amin, K. & Dannenfelser, R. M. In vitro hemolysis: Guidance for the pharmaceutical scientist. J. Pharm. Sci. 95, 1173\u20131176 (2006).","journal-title":"J. Pharm. Sci."},{"key":"95449_CR47","doi-asserted-by":"crossref","unstructured":"Mladinich, M. C., Schwedes, J. & Mackow, E. R. Zika virus persistently infects and is basolaterally released from primary human brain microvascular endothelial cells. mBio 8 (2017).","DOI":"10.1128\/mBio.00952-17"},{"key":"95449_CR48","first-page":"58","volume":"75","author":"MG Friedman","year":"1989","unstructured":"Friedman, M. G., Phillip, M. & Dagan, R. Virus-specific IgA in serum, saliva, and tears of children with measles. Clin. Exp. Immunol. 75, 58\u201363 (1989).","journal-title":"Clin. Exp. Immunol."},{"key":"95449_CR49","doi-asserted-by":"publisher","first-page":"2557","DOI":"10.3389\/fmicb.2017.02557","volume":"8","author":"MP Papa","year":"2017","unstructured":"Papa, M. P. et al. Zika virus infects, activates, and crosses brain microvascular endothelial cells, without barrier disruption. Front. Microbiol. 8, 2557 (2017).","journal-title":"Front. Microbiol."},{"key":"95449_CR50","doi-asserted-by":"publisher","first-page":"140","DOI":"10.1016\/j.antiviral.2017.02.009","volume":"141","author":"L Chen","year":"2017","unstructured":"Chen, L. et al. Antiviral activity of peptide inhibitors derived from the protein E stem against Japanese encephalitis and Zika viruses. Antiviral Res. 141, 140\u2013149 (2017).","journal-title":"Antiviral Res."},{"key":"95449_CR51","doi-asserted-by":"publisher","first-page":"148","DOI":"10.1002\/psc.2489","volume":"19","author":"S Galdiero","year":"2013","unstructured":"Galdiero, S. et al. Peptide inhibitors against herpes simplex virus infections. J. Pept. Sci. 19, 148\u2013158 (2013).","journal-title":"J. Pept. Sci."},{"key":"95449_CR52","doi-asserted-by":"publisher","first-page":"105401","DOI":"10.1016\/j.antiviral.2022.105401","volume":"207","author":"MC Mears","year":"2022","unstructured":"Mears, M. C. et al. Design and evaluation of neutralizing and fusion inhibitory peptides to Crimean-Congo hemorrhagic fever virus. Antiviral Res. 207, 105401 (2022).","journal-title":"Antiviral Res."},{"key":"95449_CR53","doi-asserted-by":"publisher","first-page":"6984","DOI":"10.1128\/JVI.00467-07","volume":"81","author":"JD Beckham","year":"2007","unstructured":"Beckham, J. D., Goody, R. J., Clarke, P., Bonny, C. & Tyler, K. L. Novel strategy for treatment of viral central nervous system infection by using a cell-permeating inhibitor of c-Jun N-terminal kinase. J. Virol. 81, 6984\u20136992 (2007).","journal-title":"J. Virol."},{"key":"95449_CR54","doi-asserted-by":"crossref","unstructured":"Yu, L. et al. Delineating antibody recognition against Zika virus during natural infection. JCI Insight 2 (2017).","DOI":"10.1172\/jci.insight.93042"},{"key":"95449_CR55","doi-asserted-by":"publisher","first-page":"e1002930","DOI":"10.1371\/journal.ppat.1002930","volume":"8","author":"SK Austin","year":"2012","unstructured":"Austin, S. K. et al. Structural basis of differential neutralization of DENV-1 genotypes by an antibody that recognizes a cryptic epitope. PLoS Pathog. 8, e1002930 (2012).","journal-title":"PLoS Pathog"},{"key":"95449_CR56","doi-asserted-by":"publisher","first-page":"1424","DOI":"10.1016\/j.celrep.2018.04.005","volume":"23","author":"C Li","year":"2018","unstructured":"Li, C. et al. A single injection of human neutralizing antibody protects against Zika virus infection and microcephaly in developing mouse embryos. Cell. Rep. 23, 1424\u20131434 (2018).","journal-title":"Cell. Rep."},{"key":"95449_CR57","doi-asserted-by":"publisher","first-page":"749","DOI":"10.1080\/22221751.2019.1614885","volume":"8","author":"X Niu","year":"2019","unstructured":"Niu, X. et al. Convalescent patient-derived monoclonal antibodies targeting different epitopes of E protein confer protection against Zika virus in a neonatal mouse model. Emerg. Microbes Infect. 8, 749\u2013759 (2019).","journal-title":"Emerg. Microbes Infect."},{"key":"95449_CR58","doi-asserted-by":"publisher","first-page":"e1000823","DOI":"10.1371\/journal.ppat.1000823","volume":"6","author":"B Shrestha","year":"2010","unstructured":"Shrestha, B. et al. The development of therapeutic antibodies that neutralize homologous and heterologous genotypes of dengue virus type 1. PLoS Pathog. 6, e1000823 (2010).","journal-title":"PLoS Pathog"},{"key":"95449_CR59","doi-asserted-by":"publisher","first-page":"229","DOI":"10.1016\/j.cell.2017.09.002","volume":"171","author":"J Wang","year":"2017","unstructured":"Wang, J. et al. A human bi-specific antibody against Zika virus with high therapeutic potential. Cell 171, 229\u2013241 e215 (2017).","journal-title":"Cell"},{"key":"95449_CR60","doi-asserted-by":"publisher","first-page":"3360","DOI":"10.1016\/j.celrep.2019.02.062","volume":"26","author":"L Wang","year":"2019","unstructured":"Wang, L. et al. Structural basis for neutralization and protection by a Zika virus-specific human antibody. Cell. Rep. 26, 3360\u20133368e3365 (2019).","journal-title":"Cell. Rep."},{"key":"95449_CR61","first-page":"665","volume":"31","author":"Y Lin","year":"2015","unstructured":"Lin, Y. et al. Mapping of the B cell neutralizing epitopes on ED III of envelope protein from dengue virus. Bing Du Xue Bao. 31, 665\u2013673 (2015).","journal-title":"Bing Du Xue Bao"},{"key":"95449_CR62","doi-asserted-by":"publisher","first-page":"155","DOI":"10.1016\/j.chom.2016.07.002","volume":"20","author":"T Tabata","year":"2016","unstructured":"Tabata, T. et al. Zika virus targets different primary human placental cells, suggesting two routes for vertical transmission. Cell. Host Microbe. 20, 155\u2013166 (2016).","journal-title":"Cell. Host Microbe"},{"key":"95449_CR63","doi-asserted-by":"publisher","first-page":"23","DOI":"10.1016\/j.peptides.2017.04.002","volume":"92","author":"K Alagarasu","year":"2017","unstructured":"Alagarasu, K. et al. In-vitro effect of human cathelicidin antimicrobial peptide LL-37 on dengue virus type 2. Peptides 92, 23\u201330 (2017).","journal-title":"Peptides"},{"key":"95449_CR64","doi-asserted-by":"publisher","first-page":"182","DOI":"10.1074\/jbc.RA118.005015","volume":"294","author":"F Li","year":"2019","unstructured":"Li, F. et al. A scorpion venom peptide Ev37 restricts viral late entry by alkalizing acidic organelles. J. Biol. Chem. 294, 182\u2013194 (2019).","journal-title":"J. Biol. Chem."},{"key":"95449_CR65","doi-asserted-by":"publisher","first-page":"79","DOI":"10.1016\/j.virol.2017.11.009","volume":"514","author":"JMC Monteiro","year":"2018","unstructured":"Monteiro, J. M. C. et al. The antimicrobial peptide HS-1 inhibits dengue virus infection. Virology 514, 79\u201387 (2018).","journal-title":"Virology"},{"key":"95449_CR66","doi-asserted-by":"crossref","unstructured":"Panya, A. et al. A synthetic bioactive peptide derived from the Asian medicinal plant acacia Catechu binds to dengue virus and inhibits cell entry. Viruses 12 (2020).","DOI":"10.3390\/v12111267"}],"container-title":["Scientific Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41598-025-95449-1.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-025-95449-1","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-025-95449-1.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,4,5]],"date-time":"2025-04-05T11:42:03Z","timestamp":1743853323000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41598-025-95449-1"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,4,3]]},"references-count":66,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2025,12]]}},"alternative-id":["95449"],"URL":"https:\/\/doi.org\/10.1038\/s41598-025-95449-1","relation":{},"ISSN":["2045-2322"],"issn-type":[{"value":"2045-2322","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,4,3]]},"assertion":[{"value":"19 November 2024","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"20 March 2025","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"3 April 2025","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"The authors declare no competing interests.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"11435"}}