{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T15:02:23Z","timestamp":1790434943252,"version":"4.1.0"},"reference-count":70,"publisher":"MDPI AG","issue":"8","license":[{"start":{"date-parts":[[2021,7,24]],"date-time":"2021-07-24T00:00:00Z","timestamp":1627084800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001381","name":"National Research Foundation Singapore","doi-asserted-by":"publisher","award":["NRF-NRFI2016-01"],"award-info":[{"award-number":["NRF-NRFI2016-01"]}],"id":[{"id":"10.13039\/501100001381","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001381","name":"National Research Foundation Singapore","doi-asserted-by":"publisher","award":["NRF2016NRF-CRP001-063"],"award-info":[{"award-number":["NRF2016NRF-CRP001-063"]}],"id":[{"id":"10.13039\/501100001381","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001381","name":"National Research Foundation Singapore","doi-asserted-by":"publisher","award":["NRF2017NRF-CRP001-027"],"award-info":[{"award-number":["NRF2017NRF-CRP001-027"]}],"id":[{"id":"10.13039\/501100001381","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Viruses"],"abstract":"<jats:p>The four serotypes of the mature dengue virus can display different morphologies, including the compact spherical, the bumpy spherical and the non-spherical clubshape morphologies. In addition, the maturation process of dengue virus is inefficient and therefore some partially immature dengue virus particles have been observed and they are infectious. All these viral particles have different antigenicity profiles and thus may affect the type of the elicited antibodies during an immune response. Understanding the molecular determinants and environmental conditions (e.g., temperature) in inducing morphological changes in the virus and how potent antibodies interact with these particles is important for designing effective therapeutics or vaccines. Several techniques, including cryoEM, site-directed mutagenesis, hydrogen-deuterium exchange mass spectrometry, time-resolve fluorescence resonance energy transfer, and molecular dynamic simulation, have been performed to investigate the structural changes. This review describes all known morphological variants of DENV discovered thus far, their surface protein dynamics and the key residues or interactions that play important roles in the structural changes.<\/jats:p>","DOI":"10.3390\/v13081446","type":"journal-article","created":{"date-parts":[[2021,7,25]],"date-time":"2021-07-25T22:07:00Z","timestamp":1627250820000},"page":"1446","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":19,"title":["Morphological Diversity and Dynamics of Dengue Virus Affecting Antigenicity"],"prefix":"10.3390","volume":"13","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9990-3335","authenticated-orcid":false,"given":"Guntur","family":"Fibriansah","sequence":"first","affiliation":[{"name":"Programme in Emerging Infectious Diseases, Duke\u2013National University of Singapore Medical School, Singapore 169857, Singapore"},{"name":"Centre for BioImaging Sciences, Department of Biological Sciences, National University of Singapore, Singapore 117557, Singapore"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xin-Ni","family":"Lim","sequence":"additional","affiliation":[{"name":"Programme in Emerging Infectious Diseases, Duke\u2013National University of Singapore Medical School, Singapore 169857, Singapore"},{"name":"Centre for BioImaging Sciences, Department of Biological Sciences, National University of Singapore, Singapore 117557, Singapore"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shee-Mei","family":"Lok","sequence":"additional","affiliation":[{"name":"Programme in Emerging Infectious Diseases, Duke\u2013National University of Singapore Medical School, Singapore 169857, Singapore"},{"name":"Centre for BioImaging Sciences, Department of Biological Sciences, National University of Singapore, Singapore 117557, Singapore"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,7,24]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"17","DOI":"10.2149\/tmh.2011-S04","article-title":"Dengue Vectors and their Spatial Distribution","volume":"39","author":"Higa","year":"2011","journal-title":"Trop. Med. Health"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1038\/nature12060","article-title":"The global distribution and burden of dengue","volume":"496","author":"Bhatt","year":"2013","journal-title":"Nature"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1358","DOI":"10.1016\/S0140-6736(14)61060-6","article-title":"Clinical efficacy and safety of a novel tetravalent dengue vaccine in healthy children in Asia: A phase 3, randomised, observer-masked, placebo-controlled trial","volume":"384","author":"Capeding","year":"2014","journal-title":"Lancet"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1056\/NEJMoa1411037","article-title":"Efficacy of a tetravalent dengue vaccine in children in Latin America","volume":"372","author":"Villar","year":"2015","journal-title":"N. Engl. J. Med."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1016\/j.ejmech.2019.05.010","article-title":"Recent update on anti-dengue drug discovery","volume":"176","author":"Dighe","year":"2019","journal-title":"Eur. J. Med. Chem."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.coviro.2020.07.009","article-title":"Recent advances in antiviral drug development towards dengue virus","volume":"43","author":"Troost","year":"2020","journal-title":"Curr. Opin. Virol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/S1567-1348(03)00004-2","article-title":"The origin, emergence and evolutionary genetics of dengue virus","volume":"3","author":"Holmes","year":"2003","journal-title":"Infect. Genet. Evol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0065-3527(08)00401-6","article-title":"The history and evolution of human dengue emergence","volume":"72","author":"Vasilakis","year":"2008","journal-title":"Adv. Virus Res."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1016\/S0140-6736(14)60572-9","article-title":"Dengue","volume":"385","author":"Guzman","year":"2015","journal-title":"Lancet"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1016\/0042-6822(90)90102-W","article-title":"Molecular evolution and distribution of dengue viruses type 1 and 2 in nature","volume":"174","year":"1990","journal-title":"Virology"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1016\/j.meegid.2009.02.003","article-title":"Molecular evolution of dengue viruses: Contributions of phylogenetics to understanding the history and epidemiology of the preeminent arboviral disease","volume":"9","author":"Weaver","year":"2009","journal-title":"Infect. Genet. Evol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1016\/S0065-3527(03)60011-4","article-title":"Neutralization and antibody-dependent enhancement of dengue viruses","volume":"60","author":"Halstead","year":"2003","journal-title":"Adv. Virus Res."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1016\/S0092-8674(02)00660-8","article-title":"Structure of dengue virus: Implications for flavivirus organization, maturation, and fusion","volume":"108","author":"Kuhn","year":"2002","journal-title":"Cell"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"7700","DOI":"10.1128\/JVI.00197-13","article-title":"Immature and mature dengue serotype 1 virus structures provide insight into the maturation process","volume":"87","author":"Kostyuchenko","year":"2013","journal-title":"J. Virol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/S0065-3527(03)59005-4","article-title":"Antigenic structure of flavivirus proteins","volume":"59","author":"Roehrig","year":"2003","journal-title":"Adv. Virus Res."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"6986","DOI":"10.1073\/pnas.0832193100","article-title":"A ligand-binding pocket in the dengue virus envelope glycoprotein","volume":"100","author":"Modis","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"11467","DOI":"10.1128\/JVI.01125-06","article-title":"Crystal structure of the West Nile virus envelope glycoprotein","volume":"80","author":"Nybakken","year":"2006","journal-title":"J. Virol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1038\/375291a0","article-title":"The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution","volume":"375","author":"Rey","year":"1995","journal-title":"Nature"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1607","DOI":"10.1016\/j.str.2004.06.019","article-title":"Conformational changes of the flavivirus E glycoprotein","volume":"12","author":"Zhang","year":"2004","journal-title":"Structure"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"2287","DOI":"10.1128\/JVI.02957-12","article-title":"Structure of a dengue virus envelope protein late-stage fusion intermediate","volume":"87","author":"Klein","year":"2013","journal-title":"J. Virol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1038\/nature02165","article-title":"Structure of the dengue virus envelope protein after membrane fusion","volume":"427","author":"Modis","year":"2004","journal-title":"Nature"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.micinf.2006.09.009","article-title":"The envelope glycoprotein domain III of dengue virus serotypes 1 and 2 inhibit virus entry","volume":"9","author":"Chin","year":"2007","journal-title":"Microbes Infect. Inst. Pasteur"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1093\/femsre\/fuu004","article-title":"Receptors and routes of dengue virus entry into the host cells","volume":"39","author":"Freire","year":"2015","journal-title":"Fems Microbiol. Rev."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1016\/j.cell.2005.11.042","article-title":"Cryo-EM reconstruction of dengue virus in complex with the carbohydrate recognition domain of DC-SIGN","volume":"124","author":"Pokidysheva","year":"2006","journal-title":"Cell"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"544","DOI":"10.1016\/j.chom.2012.08.009","article-title":"The TIM and TAM families of phosphatidylserine receptors mediate dengue virus entry","volume":"12","author":"Meertens","year":"2012","journal-title":"Cell Host Microbe."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"474","DOI":"10.1099\/vir.0.83357-0","article-title":"Functional entry of dengue virus into Aedes albopictus mosquito cells is dependent on clathrin-mediated endocytosis","volume":"89","author":"Acosta","year":"2008","journal-title":"J. Gen. Virol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"728","DOI":"10.1038\/sj.emboj.7600064","article-title":"Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation","volume":"23","author":"Bressanelli","year":"2004","journal-title":"EMBO J."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"8475","DOI":"10.1128\/jvi.71.11.8475-8481.1997","article-title":"Proteolytic activation of tick-borne encephalitis virus by furin","volume":"71","author":"Stadler","year":"1997","journal-title":"J. Virol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1099\/vir.0.18723-0","article-title":"Cleavage of protein prM is necessary for infection of BHK-21 cells by tick-borne encephalitis virus","volume":"84","author":"Elshuber","year":"2003","journal-title":"J. Gen. Virol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"2604","DOI":"10.1093\/emboj\/cdg270","article-title":"Structures of immature flavivirus particles","volume":"22","author":"Zhang","year":"2003","journal-title":"EMBO J."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1834","DOI":"10.1126\/science.1153264","article-title":"Structure of the immature dengue virus at low pH primes proteolytic maturation","volume":"319","author":"Yu","year":"2008","journal-title":"Science"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1128\/jvi.16.4.1017-1026.1975","article-title":"Dengue virus-induced modifications of host cell membranes","volume":"16","author":"Stohlman","year":"1975","journal-title":"J. Virol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"8854","DOI":"10.1074\/jbc.M512697200","article-title":"Subcellular localization and membrane topology of the Dengue virus type 2 Non-structural protein 4B","volume":"281","author":"Miller","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Tan, T.Y., Fibriansah, G., and Lok, S.M. (2020). Capsid protein is central to the birth of flavivirus particles. PLoS Pathog., 16.","DOI":"10.1371\/journal.ppat.1008542"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"895","DOI":"10.1038\/s41467-020-14647-9","article-title":"Capsid protein structure in Zika virus reveals the flavivirus assembly process","volume":"11","author":"Tan","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"2141","DOI":"10.1128\/JVI.72.3.2141-2149.1998","article-title":"Signal peptidase cleavage at the flavivirus C-prM junction: Dependence on the viral NS2B-3 protease for efficient processing requires determinants in C, the signal peptide, and prM","volume":"72","author":"Stocks","year":"1998","journal-title":"J. Virol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1152\/physiol.00005.2004","article-title":"The pH of the secretory pathway: Measurement, determinants, and regulation","volume":"19","author":"Paroutis","year":"2004","journal-title":"Physiology"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.virusres.2019.03.015","article-title":"Isolation and characterization of exosomes released from mosquito cells infected with dengue virus","volume":"266","author":"Bolanos","year":"2019","journal-title":"Virus Res."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"E6604","DOI":"10.1073\/pnas.1720125115","article-title":"Arthropod EVs mediate dengue virus transmission through interaction with a tetraspanin domain containing glycoprotein Tsp29Fb","volume":"115","author":"Vora","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"40525","DOI":"10.1074\/jbc.M112.384446","article-title":"The stem region of premembrane protein plays an important role in the virus surface protein rearrangement during dengue maturation","volume":"287","author":"Zhang","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"3269","DOI":"10.1038\/emboj.2009.245","article-title":"Structural basis for the preferential recognition of immature flaviviruses by a fusion-loop antibody","volume":"28","author":"Cherrier","year":"2009","journal-title":"EMBO J."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"8353","DOI":"10.1128\/JVI.00696-10","article-title":"Influence of pr-M cleavage on the heterogeneity of extracellular dengue virus particles","volume":"84","author":"Junjhon","year":"2010","journal-title":"J. Virol."},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Richter, M.K., da Silva Voorham, J.M., Torres Pedraza, S., Hoornweg, T.E., van de Pol, D.P., Rodenhuis-Zybert, I.A., Wilschut, J., and Smit, J.M. (2014). Immature dengue virus is infectious in human immature dendritic cells via interaction with the receptor molecule DC-SIGN. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0098785"},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Rodenhuis-Zybert, I.A., van der Schaar, H.M., da Silva Voorham, J.M., van der Ende-Metselaar, H., Lei, H.Y., Wilschut, J., and Smit, J.M. (2010). Immature dengue virus: A veiled pathogen?. PLoS Pathog., 6.","DOI":"10.1371\/journal.ppat.1000718"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/j.str.2018.10.009","article-title":"Mechanism of Enhanced Immature Dengue Virus Attachment to Endosomal Membrane Induced by prM Antibody","volume":"27","author":"Wirawan","year":"2019","journal-title":"Structure"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"7585","DOI":"10.1128\/JVI.00757-13","article-title":"Structural changes in dengue virus when exposed to a temperature of 37 degrees C","volume":"87","author":"Fibriansah","year":"2013","journal-title":"J. Virol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"3112","DOI":"10.1038\/s41467-020-16925-y","article-title":"High flavivirus structural plasticity demonstrated by a non-spherical morphological variant","volume":"11","author":"Morrone","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"6141","DOI":"10.1128\/JVI.00037-07","article-title":"Structure of immature West Nile virus","volume":"81","author":"Zhang","year":"2007","journal-title":"J. Virol."},{"key":"ref_49","doi-asserted-by":"crossref","unstructured":"Newton, N.D., Hardy, J.M., Modhiran, N., Hugo, L.E., Amarilla, A.A., Bibby, S., Venugopal, H., Harrison, J.J., Traves, R.J., and Hall, R.A. (2021). The structure of an infectious immature flavivirus redefines viral architecture and maturation. Sci. Adv., 7.","DOI":"10.1126\/sciadv.abe4507"},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Fibriansah, G., Lim, E.X.Y., Marzinek, J.K., Ng, T.S., Tan, J.L., Huber, R.G., Lim, X.N., Chew, V.S.Y., Kostyuchenko, V.A., and Shi, J. (2021). Antibody affinity versus dengue morphology influences neutralization. PLoS Pathog., 17.","DOI":"10.1371\/journal.ppat.1009331"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1128\/JVI.02641-13","article-title":"Near-atomic resolution cryo-electron microscopic structure of dengue serotype 4 virus","volume":"88","author":"Kostyuchenko","year":"2014","journal-title":"J. Virol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1038\/nsmb.2463","article-title":"Cryo-EM structure of the mature dengue virus at 3.5-A resolution","volume":"20","author":"Zhang","year":"2013","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"6341","DOI":"10.1038\/ncomms7341","article-title":"A highly potent human antibody neutralizes dengue virus serotype 3 by binding across three surface proteins","volume":"6","author":"Fibriansah","year":"2015","journal-title":"Nat. Commun."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1038\/nature17994","article-title":"Structure of the thermally stable Zika virus","volume":"533","author":"Kostyuchenko","year":"2016","journal-title":"Nature"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1016\/j.jsb.2013.04.005","article-title":"Membrane curvature in flaviviruses","volume":"183","author":"Zhang","year":"2013","journal-title":"J. Struct. Biol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"3266","DOI":"10.1038\/s41467-021-22773-1","article-title":"A unified route for flavivirus structures uncovers essential pocket factors conserved across pathogenic viruses","volume":"12","author":"Hardy","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"6795","DOI":"10.1073\/pnas.1304300110","article-title":"Dengue structure differs at the temperatures of its human and mosquito hosts","volume":"110","author":"Zhang","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Lim, X.N., Shan, C., Marzinek, J.K., Dong, H., Ng, T.S., Ooi, J.S.G., Fibriansah, G., Wang, J., Verma, C.S., and Bond, P.J. (2019). Molecular basis of dengue virus serotype 2 morphological switch from 29 degrees C to 37 degrees C. PLoS Pathog., 15.","DOI":"10.1371\/journal.ppat.1007996"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1126\/science.aaa8651","article-title":"DENGUE VIRUS. Cryo-EM structure of an antibody that neutralizes dengue virus type 2 by locking E protein dimers","volume":"349","author":"Fibriansah","year":"2015","journal-title":"Science"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"14339","DOI":"10.1038\/ncomms14339","article-title":"Conformational changes in intact dengue virus reveal serotype-specific expansion","volume":"8","author":"Lim","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"13679","DOI":"10.1038\/ncomms13679","article-title":"Neutralization mechanism of a highly potent antibody against Zika virus","volume":"7","author":"Zhang","year":"2016","journal-title":"Nat. Commun."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"358","DOI":"10.1002\/emmm.201303404","article-title":"A potent anti-dengue human antibody preferentially recognizes the conformation of E protein monomers assembled on the virus surface","volume":"6","author":"Fibriansah","year":"2014","journal-title":"EMBO Mol. Med."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"139ra183","DOI":"10.1126\/scitranslmed.3003888","article-title":"The structural basis for serotype-specific neutralization of dengue virus by a human antibody","volume":"4","author":"Teoh","year":"2012","journal-title":"Sci. Transl. Med."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.virol.2013.01.022","article-title":"The mechanism of differential neutralization of dengue serotype 3 strains by monoclonal antibody 8A1","volume":"439","author":"Zhou","year":"2013","journal-title":"Virology"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"7439","DOI":"10.1073\/pnas.1200566109","article-title":"Identification of human neutralizing antibodies that bind to complex epitopes on dengue virions","volume":"109","author":"Smith","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1038\/ni.3058","article-title":"A new class of highly potent, broadly neutralizing antibodies isolated from viremic patients infected with dengue virus","volume":"16","author":"Dejnirattisai","year":"2015","journal-title":"Nat. Immunol."},{"key":"ref_67","doi-asserted-by":"crossref","unstructured":"Rouvinski, A., Guardado-Calvo, P., Barba-Spaeth, G., Duquerroy, S., Vaney, M.C., Kikuti, C.M., Navarro Sanchez, M.E., Dejnirattisai, W., Wongwiwat, W., and Haouz, A. (2015). Recognition determinants of broadly neutralizing human antibodies against dengue viruses. Nature.","DOI":"10.1038\/nature14130"},{"key":"ref_68","doi-asserted-by":"crossref","unstructured":"Dowd, K.A., Jost, C.A., Durbin, A.P., Whitehead, S.S., and Pierson, T.C. (2011). A dynamic landscape for antibody binding modulates antibody-mediated neutralization of West Nile virus. PLoS Pathog., 7.","DOI":"10.1371\/journal.ppat.1002111"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1038\/nsmb.1382","article-title":"Binding of a neutralizing antibody to dengue virus alters the arrangement of surface glycoproteins","volume":"15","author":"Lok","year":"2008","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"12562","DOI":"10.1128\/JVI.00871-13","article-title":"High-avidity and potently neutralizing cross-reactive human monoclonal antibodies derived from secondary dengue virus infection","volume":"87","author":"Tsai","year":"2013","journal-title":"J. Virol."}],"container-title":["Viruses"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1999-4915\/13\/8\/1446\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T06:34:34Z","timestamp":1760164474000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1999-4915\/13\/8\/1446"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,7,24]]},"references-count":70,"journal-issue":{"issue":"8","published-online":{"date-parts":[[2021,8]]}},"alternative-id":["v13081446"],"URL":"https:\/\/doi.org\/10.3390\/v13081446","relation":{},"ISSN":["1999-4915"],"issn-type":[{"value":"1999-4915","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,7,24]]}}}