Monath TP, 1986. Pathobiology of the flaviviruses. Schlesinger S, Schlesinger MJ, eds. The Togaviridae and Flaviviridae. New York, NY: Plenum Press, 375–440.
Halstead SB, 2006. Dengue in the Americas and southeast Asia: do they differ? Rev Panam Salud Publica 20: 407–415.
Simmons M, 2012. Advances in the development of vaccines for dengue fever. Vaccine (Auckl) 2: 1–14.
Kanesa-Thasan N, Sun W, Kim-Ahn G, Van Albert S, Putnak J, King A, Raengsakulsrach B, Christ-Schmidt H, Gilson K, Zahradnik J, 2001. Safety and immunogenicity of attenuated dengue virus vaccines (Aventis Pasteur) in human volunteers. Vaccine 19: 3179–3188.
Kanesa-Thasan N, Edelman R, Tacket CO, Wasserman SS, Vaughn DW, Coster TS, Kim-Ahn GJ, Dubois DR, Putnak JR, King A, Summers PL, Innis BL, Eckels KH, Hoke CH Jr, 2003. Phase 1 studies of Walter Reed Army Institute of Research candidate attenuated dengue vaccines: selection of safe and immunogenic monovalent vaccines. Am J Trop Med Hyg 69: 17–23.
Sabchareon A, Lang J, Chanthavanich P, Yoksan S, Forrat R, Attanath P, Sirivichayakul C, Pengsaa K, Pojjaroen-Anant C, Chambonneau L, Saluzzo JF, Bhamarapravati N, 2004. Safety and immunogenicity of a three dose regimen of two tetravalent live-attenuated dengue vaccines in five- to twelve-year-old Thai children. Pediatr Infect Dis J 23: 99–109.
Hadinegoro SR, Arredondo-García JL, Capeding MR, Deseda C, Chotpitayasunondh T, Dietze R, Hj Muhammad Ismail H, Reynales H, Limkittikul K, Rivera-Medina DM, 2015. Efficacy and long-term safety of a dengue vaccine in regions of endemic disease. N Engl J Med 373: 1195–1206.
Casadevall A, 2002. Passive antibody administration (immediate immunity) as a specific defense against biological weapons. Emerg Infect Dis 8: 833–842.
Leung AK, Kellner JD, Davies HD, 2005. Hepatitis A: a preventable threat. Adv Ther 22: 578–586.
Blaise A, Gautret P, 2015. Current perspectives on rabies postexposure prophylaxis. Infect Disord Drug Targets 15: 13–19.
Halstead SB, 2003. Neutralization and antibody-dependent enhancement of dengue viruses. Adv Virus Res 60: 421–467.
Burke DS, Kliks S, 2006. Antibody-dependent enhancement in dengue virus infections. J Infect Dis 193: 601–603, author reply 603–604.
Kliks SC, Nisalak A, Brandt WE, Wahl L, Burke DS, 1989. Antibody-dependent enhancement of dengue virus growth in human monocytes as a risk factor for dengue hemorrhagic fever. Am J Trop Med Hyg 40: 444–451.
Sarvas H, Seppälä I, Kurikka S, Siegberg R, Mäkelä O, 1993. Half-life of the maternal IgG1 allotype in infants. J Clin Immunol 13: 145–151.
Robbie GJ, Criste R, Dall'acqua WF, Jensen K, Patel NK, Losonsky GA, Griffin MP, 2013. A novel investigational Fc-modified humanized monoclonal antibody, motavizumab-YTE, has an extended half-life in healthy adults. Antimicrob Agents Chemother 57: 6147–6153.
Woodle ES, Xu D, Zivin RA, Auger J, Charette J, O'Laughlin R, Peace D, Jollife LK, Haverty T, Bluestone JA, Thistlethwaite JR Jr, 1999. Phase I trial of a humanized, Fc receptor nonbinding OKT3 antibody, huOKT3γ1 (Ala-Ala) in the treatment of acute renal allograft rejection. Transplantation 68: 608–616.
Herold KC, Gitelman SE, Masharani U, Hagopian W, Bisikirska B, Donaldson D, Rother K, Diamond B, Harlan DM, Bluestone JA, 2005. A single course of anti-CD3 monoclonal antibody hOKT3γ1 (Ala-Ala) results in improvement in C-peptide responses and clinical parameters for at least 2 years after onset of type 1 diabetes. Diabetes 54: 1763–1769.
Haigwood NL, Montefiori DC, Sutton WF, McClure J, Watson AJ, Voss G, Hirsch VM, Richardson BA, Letvin NL, Hu S-L, 2004. Passive immunotherapy in simian immunodeficiency virus-infected macaques accelerates the development of neutralizing antibodies. J Virol 78: 5983–5995.
Zhang L, Ribeiro RM, Mascola JR, Lewis MG, Stiegler G, Katinger H, Perelson AS, Davenport MP, 2004. Effects of antibody on viral kinetics in simian/human immunodeficiency virus infection: implications for vaccination. J Virol 78: 5520–5522.
Gupta M, Mahanty S, Bray M, Ahmed R, Rollin PE, 2001. Passive transfer of antibodies protects immunocompetent and immunodeficient mice against lethal Ebola virus infection without complete inhibition of viral replication. J Virol 75: 4649–4654.
Jahrling P, Geisbert J, Swearengen J, Jaax G, Lewis T, Huggins J, Schmidt J, LeDuc J, Peters C, 1996. Passive immunization of Ebola virus-infected cynomolgus monkeys with immunoglobulin from hyperimmune horses. Arch Virol Suppl 11: 135–140.
Marasco WA, Sui J, 2007. The growth and potential of human antiviral monoclonal antibody therapeutics. Nat Biotechnol 25: 1421–1434.
Kudoyarova-Zubavichene NM, Sergeyev NN, Chepurnov AA, Netesov SV, 1999. Preparation and use of hyperimmune serum for prophylaxis and therapy of Ebola virus infections. J Infect Dis 179: S218–S223.
Kaufman B, Summers P, Dubois D, Cohen WH, Gentry M, Timchak RL, Burke DS, Eckels KH, 1989. Monoclonal antibodies for dengue virus prM glycoprotein protect mice against lethal dengue infection. Am J Trop Med Hyg 41: 576–580.
Kaufman B, Summers P, Dubois D, Eckels K, 1987. Monoclonal antibodies against dengue 2 virus E-glycoprotein protect mice against lethal dengue infection. Am J Trop Med Hyg 36: 427–434.
Henchal E, Henchal L, Schlesinger J, 1988. Synergistic interactions of anti-NS1 monoclonal antibodies protect passively immunized mice from lethal challenge with dengue 2 virus. J Gen Virol 69: 2101–2107.
Pickering LK, 2003. Red Book: 2003 Report of the Committee on Infectious Diseases. Elk Grove Village, IL: American Academy of Pediatrics.
Avnir Y, Tallarico AS, Zhu Q, Bennett AS, Connelly G, Sheehan J, Sui J, Fahmy A, Huang C, Cadwell G, 2014. Molecular signatures of hemagglutinin stem-directed heterosubtypic human neutralizing antibodies against influenza A viruses. PLoS Pathog 10: e1004103.
Balsitis SJ, Williams KL, Lachica R, Flores D, Kyle JL, Mehlhop E, Johnson S, Diamond MS, Beatty PR, Harris E, 2010. Lethal antibody enhancement of dengue disease in mice is prevented by Fc modification. PLoS Pathog 6: e1000790.
Sultana H, Foellmer HG, Neelakanta G, Oliphant T, Engle M, Ledizet M, Krishnan MN, Bonafé N, Anthony KG, Marasco WA, 2009. Fusion loop peptide of the West Nile virus envelope protein is essential for pathogenesis and is recognized by a therapeutic cross-reactive human monoclonal antibody. J Immunol 183: 650–660.
Hessell AJ, Hangartner L, Hunter M, Havenith CE, Beurskens FJ, Bakker JM, Lanigan CM, Landucci G, Forthal DN, Parren PW, Marx PA, Burton DR, 2007. Fc receptor but not complement binding is important in antibody protection against HIV. Nature 449: 101–104.
Simmons M, Nelson WM, Wu S, Hayes CG, 1998. Evaluation of the protective efficacy of a recombinant dengue envelope B domain fusion protein against dengue 2 virus infection in mice. Am J Trop Med Hyg 58: 655–662.
Russell PK, Nisalak A, 1967. Dengue virus identification by the plaque reduction neutralization test. J Immunol 99: 291–296.
Goncalvez AP, Engle RE, Claire MS, Purcell RH, Lai C-J, 2007. Monoclonal antibody-mediated enhancement of dengue virus infection in vitro and in vivo and strategies for prevention. Proc Natl Acad Sci USA 104: 9422–9427.
Eckels KH, Brandt WE, Harrison VR, McCown JM, Russell PK, 1976. Isolation of a temperature-sensitive dengue-2 virus under conditions suitable for vaccine development. Infect Immun 14: 1221–1227.
Simmons M, Porter KR, Hayes CG, Vaughn DW, Putnak R, 2006. Characterization of antibody responses to combinations of a dengue virus type 2 DNA vaccine and two dengue virus type 2 protein vaccines in rhesus macaques. J Virol 80: 9577–9585.
Simmons M, Burgess T, Lynch J, Putnak R, 2010. Protection against dengue virus by non-replicating and live attenuated vaccines used together in a prime boost vaccination strategy. Virology 396: 280–288.
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Passive immunization with anti-dengue virus (DENV) immune serum globulin (ISG) or monoclonal antibodies (Mabs) may serve to supplement or replace vaccination for short-term dengue immune prophylaxis. In the present study, we sought to establish proof-of-concept by evaluating several DENV-neutralizing antibodies for their ability to protect rhesus macaques against viremia following live virus challenge, including human anti-dengue ISG, and a human Mab (Mab11/wt) and its genetically engineered variant (Mab11/mutFc) that is unable to bind to cells with Fc gamma receptors (FcγR) and potentiate antibody-dependent enhancement (ADE). In the first experiment, groups of animals received ISG or Mab11/wt at low doses (3–10 mg/kg) or a saline control followed by challenge with DENV-2 at day 10 or 30. After passive immunization, only low-titered circulating virus-neutralizing antibody titers were measured in both groups, which were undetectable by day 30. After challenge at day 10, a reduction in viremia duration compared with the control was seen only in the ISG group (75%). However, after a day 30 challenge, no reduction in viremia was observed in both immunized groups. In a second experiment to test the effect of higher antibody doses on short-term protection, groups received either ISG, Mab11/wt, Mab11/mutFc (each at 25 mg/kg) or saline followed by challenge with DENV-2 on day 10. Increased virus-neutralizing antibody titers were detected in all groups at day 5 postinjection, with geometric mean titers (GMTs) of 464 (ISG), 313 (Mab11/wt), and 309 (Mab11/mutFc). After challenge, there was complete protection against viremia in the group that received ISG, and a reduction in viremia duration of 89% and 83% in groups that received Mab11/wt and Mab11/mutFc, respectively. An in vitro ADE assay in Fcγ receptor-bearing K562 cells with sera collected immediately before challenge showed increased DENV-2 infection levels in the presence of both ISG and Mab11/wt, which peaked at a serum dilution of 1:90, but not in Mab11/mutFc containing sera. The results suggest that antibody prophylaxis for dengue might be beneficial in eliminating or reducing viral loads thereby minimizing disease progression. Our results also suggest that blocking FcγR interactions through Mab11 Fc engineering may further prevent ADE.
Conflict of interest: Wayne A. Marasco is an inventor on a provisional patent entitled, “Flavivirus neutralizing antibodies and methods of use thereof” that is owned by the Dana-Farber Cancer Institute and covers the monoclonal antibody used in these studies. Monika Simmons, Robert Putnak, and Timothy Burgess are employees of the U.S. Government.
Financial support: This work was funded by a grant from the Military Infectious Disease Research Program (MIDRP), U.S. Army Medical Research and Materiel Command, Fort Detrick, MD, work unit number A0311.
Copyright statement: This work was prepared as part of our official duties. Title 17 U.S.C. article 105 provides that “Copyright protection under this title is not available for any work of the United States Government.” Title 17 U.S.C. article 101 defines a U.S. Government work as a work prepared by a military service member or employee of the U.S. Government as part of that person's official duties.
Authors' addresses: Monika Simmons and Peifang Sun, Naval Medical Research Center (NMRC), Silver Spring, MD, E-mails: firstname.lastname@example.org and email@example.com. Robert Putnak, Walter Reed Army Institute of Research (WRAIR), Silver Spring, MD, E-mail: firstname.lastname@example.org. Timothy Burgess, Infectious Diseases Service, Walter Reed National Military Medical Center (WRNMMC), Bethesda, MD, E-mail: email@example.com. Wayne A. Marasco, Dana Farber Cancer Institute, Harvard Medical School, Boston, MA, E-mail: wayne_Marasco@dfci.harvard.edu.