A Cross-Reactive Humanized Monoclonal Antibody Targeting Fusion Glycoprotein Function Protects Ferrets Against Lethal Nipah Virus and Hendra Virus Infection
Abstract Background Nipah virus (NiV) and Hendra virus (HeV) are zoonotic paramyxoviruses that cause severe disease in both animals and humans. There are no approved vaccines or treatments for use in humans; however, therapeutic treatment of both NiV and HeV infection in ferrets and non-human primat...
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| Published in | The Journal of infectious diseases Vol. 221; no. Supplement_4; pp. S471 - S479 |
|---|---|
| Main Authors | , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
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Oxford University Press
11.05.2020
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| Abstract | Abstract
Background
Nipah virus (NiV) and Hendra virus (HeV) are zoonotic paramyxoviruses that cause severe disease in both animals and humans. There are no approved vaccines or treatments for use in humans; however, therapeutic treatment of both NiV and HeV infection in ferrets and non-human primates with a cross-reactive, neutralizing human monoclonal antibody (mAb), m102.4, targeting the G glycoprotein has been demonstrated. In a previous study, we isolated, characterized, and humanized a cross-reactive, neutralizing anti-F mAb (h5B3.1). The mAb h5B3.1 blocks the required F conformational change needed to facilitate membrane fusion and virus infection, and the epitope recognized by h5B3.1 has been structurally defined; however, the efficacy of h5B3.1 in vivo is unknown.
Methods
The post-infection antiviral activity of h5B3.1 was evaluated in vivo by administration in ferrets after NiV and HeV virus challenge.
Results
All subjects that received h5B3.1 from 1 to several days after infection with a high-dose, oral-nasal virus challenge were protected from disease, whereas all controls died.
Conclusions
This is the first successful post-exposure antibody therapy for NiV and HeV using a humanized cross-reactive mAb targeting the F glycoprotein, and the findings suggest that a combination therapy targeting both F and G should be evaluated as a therapy for NiV/HeV infection. |
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| AbstractList | Abstract
Background
Nipah virus (NiV) and Hendra virus (HeV) are zoonotic paramyxoviruses that cause severe disease in both animals and humans. There are no approved vaccines or treatments for use in humans; however, therapeutic treatment of both NiV and HeV infection in ferrets and non-human primates with a cross-reactive, neutralizing human monoclonal antibody (mAb), m102.4, targeting the G glycoprotein has been demonstrated. In a previous study, we isolated, characterized, and humanized a cross-reactive, neutralizing anti-F mAb (h5B3.1). The mAb h5B3.1 blocks the required F conformational change needed to facilitate membrane fusion and virus infection, and the epitope recognized by h5B3.1 has been structurally defined; however, the efficacy of h5B3.1 in vivo is unknown.
Methods
The post-infection antiviral activity of h5B3.1 was evaluated in vivo by administration in ferrets after NiV and HeV virus challenge.
Results
All subjects that received h5B3.1 from 1 to several days after infection with a high-dose, oral-nasal virus challenge were protected from disease, whereas all controls died.
Conclusions
This is the first successful post-exposure antibody therapy for NiV and HeV using a humanized cross-reactive mAb targeting the F glycoprotein, and the findings suggest that a combination therapy targeting both F and G should be evaluated as a therapy for NiV/HeV infection. Nipah virus (NiV) and Hendra virus (HeV) are zoonotic paramyxoviruses that cause severe disease in both animals and humans. There are no approved vaccines or treatments for use in humans; however, therapeutic treatment of both NiV and HeV infection in ferrets and non-human primates with a cross-reactive, neutralizing human monoclonal antibody (mAb), m102.4, targeting the G glycoprotein has been demonstrated. In a previous study, we isolated, characterized, and humanized a cross-reactive, neutralizing anti-F mAb (h5B3.1). The mAb h5B3.1 blocks the required F conformational change needed to facilitate membrane fusion and virus infection, and the epitope recognized by h5B3.1 has been structurally defined; however, the efficacy of h5B3.1 in vivo is unknown. The post-infection antiviral activity of h5B3.1 was evaluated in vivo by administration in ferrets after NiV and HeV virus challenge. All subjects that received h5B3.1 from 1 to several days after infection with a high-dose, oral-nasal virus challenge were protected from disease, whereas all controls died. This is the first successful post-exposure antibody therapy for NiV and HeV using a humanized cross-reactive mAb targeting the F glycoprotein, and the findings suggest that a combination therapy targeting both F and G should be evaluated as a therapy for NiV/HeV infection. Background Nipah virus (NiV) and Hendra virus (HeV) are zoonotic paramyxoviruses that cause severe disease in both animals and humans. There are no approved vaccines or treatments for use in humans; however, therapeutic treatment of both NiV and HeV infection in ferrets and non-human primates with a cross-reactive, neutralizing human monoclonal antibody (mAb), m102.4, targeting the G glycoprotein has been demonstrated. In a previous study, we isolated, characterized, and humanized a cross-reactive, neutralizing anti-F mAb (h5B3.1). The mAb h5B3.1 blocks the required F conformational change needed to facilitate membrane fusion and virus infection, and the epitope recognized by h5B3.1 has been structurally defined; however, the efficacy of h5B3.1 in vivo is unknown. Methods The post-infection antiviral activity of h5B3.1 was evaluated in vivo by administration in ferrets after NiV and HeV virus challenge. Results All subjects that received h5B3.1 from 1 to several days after infection with a high-dose, oral-nasal virus challenge were protected from disease, whereas all controls died. Conclusions This is the first successful post-exposure antibody therapy for NiV and HeV using a humanized cross-reactive mAb targeting the F glycoprotein, and the findings suggest that a combination therapy targeting both F and G should be evaluated as a therapy for NiV/HeV infection. Nipah virus (NiV) and Hendra virus (HeV) are zoonotic paramyxoviruses that cause severe disease in both animals and humans. There are no approved vaccines or treatments for use in humans; however, therapeutic treatment of both NiV and HeV infection in ferrets and non-human primates with a cross-reactive, neutralizing human monoclonal antibody (mAb), m102.4, targeting the G glycoprotein has been demonstrated. In a previous study, we isolated, characterized, and humanized a cross-reactive, neutralizing anti-F mAb (h5B3.1). The mAb h5B3.1 blocks the required F conformational change needed to facilitate membrane fusion and virus infection, and the epitope recognized by h5B3.1 has been structurally defined; however, the efficacy of h5B3.1 in vivo is unknown.BACKGROUNDNipah virus (NiV) and Hendra virus (HeV) are zoonotic paramyxoviruses that cause severe disease in both animals and humans. There are no approved vaccines or treatments for use in humans; however, therapeutic treatment of both NiV and HeV infection in ferrets and non-human primates with a cross-reactive, neutralizing human monoclonal antibody (mAb), m102.4, targeting the G glycoprotein has been demonstrated. In a previous study, we isolated, characterized, and humanized a cross-reactive, neutralizing anti-F mAb (h5B3.1). The mAb h5B3.1 blocks the required F conformational change needed to facilitate membrane fusion and virus infection, and the epitope recognized by h5B3.1 has been structurally defined; however, the efficacy of h5B3.1 in vivo is unknown.The post-infection antiviral activity of h5B3.1 was evaluated in vivo by administration in ferrets after NiV and HeV virus challenge.METHODSThe post-infection antiviral activity of h5B3.1 was evaluated in vivo by administration in ferrets after NiV and HeV virus challenge.All subjects that received h5B3.1 from 1 to several days after infection with a high-dose, oral-nasal virus challenge were protected from disease, whereas all controls died.RESULTSAll subjects that received h5B3.1 from 1 to several days after infection with a high-dose, oral-nasal virus challenge were protected from disease, whereas all controls died.This is the first successful post-exposure antibody therapy for NiV and HeV using a humanized cross-reactive mAb targeting the F glycoprotein, and the findings suggest that a combination therapy targeting both F and G should be evaluated as a therapy for NiV/HeV infection.CONCLUSIONSThis is the first successful post-exposure antibody therapy for NiV and HeV using a humanized cross-reactive mAb targeting the F glycoprotein, and the findings suggest that a combination therapy targeting both F and G should be evaluated as a therapy for NiV/HeV infection. |
| Author | Borisevich, Viktoriya Broder, Christopher C Dang, Ha V Veesler, David Fenton, Karla A Cross, Robert W Mire, Chad E Chan, Yee-Peng Geisbert, Thomas W Yan, Lianying Agans, Krystle N |
| AuthorAffiliation | 3 Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences , Bethesda, Maryland, USA 4 Department of Biochemistry, University of Washington , Seattle, Washington, USA 1 Galveston National Laboratory, University of Texas Medical Branch , Galveston, Texas, USA 2 Department of Microbiology and Immunology , University of Texas Medical Branch , Galveston, Texas, USA |
| AuthorAffiliation_xml | – name: 3 Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences , Bethesda, Maryland, USA – name: 4 Department of Biochemistry, University of Washington , Seattle, Washington, USA – name: 2 Department of Microbiology and Immunology , University of Texas Medical Branch , Galveston, Texas, USA – name: 1 Galveston National Laboratory, University of Texas Medical Branch , Galveston, Texas, USA |
| Author_xml | – sequence: 1 givenname: Chad E surname: Mire fullname: Mire, Chad E organization: Galveston National Laboratory, University of Texas Medical Branch, Galveston, Texas, USA – sequence: 2 givenname: Yee-Peng surname: Chan fullname: Chan, Yee-Peng organization: Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, Bethesda, Maryland, USA – sequence: 3 givenname: Viktoriya surname: Borisevich fullname: Borisevich, Viktoriya organization: Galveston National Laboratory, University of Texas Medical Branch, Galveston, Texas, USA – sequence: 4 givenname: Robert W surname: Cross fullname: Cross, Robert W organization: Galveston National Laboratory, University of Texas Medical Branch, Galveston, Texas, USA – sequence: 5 givenname: Lianying surname: Yan fullname: Yan, Lianying organization: Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, Bethesda, Maryland, USA – sequence: 6 givenname: Krystle N surname: Agans fullname: Agans, Krystle N organization: Galveston National Laboratory, University of Texas Medical Branch, Galveston, Texas, USA – sequence: 7 givenname: Ha V surname: Dang fullname: Dang, Ha V organization: Department of Biochemistry, University of Washington, Seattle, Washington, USA – sequence: 8 givenname: David surname: Veesler fullname: Veesler, David organization: Department of Biochemistry, University of Washington, Seattle, Washington, USA – sequence: 9 givenname: Karla A surname: Fenton fullname: Fenton, Karla A organization: Galveston National Laboratory, University of Texas Medical Branch, Galveston, Texas, USA – sequence: 10 givenname: Thomas W surname: Geisbert fullname: Geisbert, Thomas W organization: Galveston National Laboratory, University of Texas Medical Branch, Galveston, Texas, USA – sequence: 11 givenname: Christopher C surname: Broder fullname: Broder, Christopher C email: christopher.broder@usuhs.edu organization: Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, Bethesda, Maryland, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/31686101$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1371/journal.ppat.1003684 10.1016/j.chom.2018.12.005 10.1016/j.chom.2018.12.004 10.4269/ajtmh.2011.10-0567 10.1016/j.coviro.2014.01.005 10.3201/eid2102.141433 10.1086/651022 10.1186/1743-422X-10-237 10.1038/s41594-019-0308-9 10.1016/j.vaccine.2011.06.015 10.1038/srep30916 10.1016/j.coviro.2016.02.004 10.1007/978-1-4614-7651-1_6 10.1371/journal.pntd.0004775 10.1128/JVI.01318-12 10.1038/nature13777 10.1126/science.288.5470.1432 10.1186/s12992-017-0233-9 10.3201/eid1202.051247 10.1099/0022-1317-81-8-1927 10.1128/JVI.80.4.1972-1978.2006 10.1073/pnas.1523303113 10.1016/j.vaccine.2016.03.075 10.3201/eid1012.040701 10.1016/j.tvjl.2008.10.016 10.1073/pnas.0504887102 10.1128/JVI.80.2.891-899.2006 10.1086/528801 10.1126/scitranslmed.3008929 10.1371/journal.pntd.0006343 10.1038/ncomms8483 10.3201/eid2501.180267 10.1371/journal.ppat.1000642 10.1038/nrmicro974 10.1016/S1286-4579(01)01522-2 10.1016/j.virol.2009.03.001 10.1038/nature03838 10.1126/scitranslmed.3002901 |
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| Copyright | Published by Oxford University Press for the Infectious Diseases Society of America 2019. 2019 Published by Oxford University Press for the Infectious Diseases Society of America 2019. |
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| References | Bossart (2020051111580570200_CIT0028) 2011; 3 Bossart (2020051111580570200_CIT0025) 2009; 5 Rubin (2020051111580570200_CIT0038) 2013 Wec (2020051111580570200_CIT0044) 2019; 25 Broder (2020051111580570200_CIT0021) 2012; 359 Broder (2020051111580570200_CIT0010) 2016; 34 Qiu (2020051111580570200_CIT0046) 2014; 514 Rockx (2020051111580570200_CIT0047) 2010; 201 Wang (2020051111580570200_CIT0001) 2013 Chadha (2020051111580570200_CIT0012) 2006; 12 Dang (2020051111580570200_CIT0031) 2019 Casadevall (2020051111580570200_CIT0040) 2004; 2 (2020051111580570200_CIT0009) 2019 Bornholdt (2020051111580570200_CIT0045) 2019; 25 Halpin (2020051111580570200_CIT0005) 2000; 81 Xu (2020051111580570200_CIT0022) 2013; 9 Griffin (2020051111580570200_CIT0039) 2013 Negrete (2020051111580570200_CIT0020) 2005; 436 Satterfield (2020051111580570200_CIT0036) 2015; 6 Bonaparte (2020051111580570200_CIT0019) 2005; 102 Guillaume (2020051111580570200_CIT0041) 2009; 387 Geisbert (2020051111580570200_CIT0002) 2012; 359 Wong (2020051111580570200_CIT0030) 2016; 113 Clayton (2020051111580570200_CIT0032) 2016; 10 Pallister (2020051111580570200_CIT0035) 2013; 10 Wong (2020051111580570200_CIT0016) 2011; 2011 Pallister (2020051111580570200_CIT0034) 2011; 29 Geisbert (2020051111580570200_CIT0027) 2014; 6 Sweileh (2020051111580570200_CIT0015) 2017; 13 Chua (2020051111580570200_CIT0011) 2000; 288 Bossart (2020051111580570200_CIT0018) 2013; 790 Anderson (2020051111580570200_CIT0007) 2019; 25 Zhu (2020051111580570200_CIT0023) 2006; 80 Hsu (2020051111580570200_CIT0013) 2004; 10 Chan (2020051111580570200_CIT0029) 2012; 86 Field (2020051111580570200_CIT0004) 2016; 16 Chua (2020051111580570200_CIT0006) 2002; 4 Karron (2020051111580570200_CIT0037) 2013 Halpin (2020051111580570200_CIT0003) 2011; 85 Zhu (2020051111580570200_CIT0024) 2008; 197 Ching (2020051111580570200_CIT0014) 2015; 21 Guillaume (2020051111580570200_CIT0042) 2006; 80 (2020051111580570200_CIT0008) 2018 Jardetzky (2020051111580570200_CIT0043) 2014; 5 Weingartl (2020051111580570200_CIT0017) 2009; 181 Mire (2020051111580570200_CIT0026) 2016; 6 Leon (2020051111580570200_CIT0033) 2018; 12 |
| References_xml | – volume: 2011 start-page: 567248 year: 2011 ident: 2020051111580570200_CIT0016 article-title: Pathology of acute henipavirus infection in humans and animals publication-title: Patholog Res Int – volume: 9 start-page: e1003684 year: 2013 ident: 2020051111580570200_CIT0022 article-title: Crystal structure of the Hendra virus attachment G glycoprotein bound to a potent cross-reactive neutralizing human monoclonal antibody publication-title: PLoS Pathog doi: 10.1371/journal.ppat.1003684 – volume: 25 start-page: 49 year: 2019 ident: 2020051111580570200_CIT0045 article-title: A two-antibody pan-ebolavirus cocktail confers broad therapeutic protection in ferrets and nonhuman primates publication-title: Cell Host Microbe doi: 10.1016/j.chom.2018.12.005 – volume-title: Summary of Hendra virus incidents in horses year: 2019 ident: 2020051111580570200_CIT0009 – start-page: 1024 volume-title: Fields Virology year: 2013 ident: 2020051111580570200_CIT0038 article-title: Mumps virus – volume: 25 start-page: 39 year: 2019 ident: 2020051111580570200_CIT0044 article-title: Development of a human antibody cocktail that deploys multiple functions to confer pan-ebolavirus protection publication-title: Cell Host Microbe doi: 10.1016/j.chom.2018.12.004 – start-page: 1070 volume-title: Fields Virology year: 2013 ident: 2020051111580570200_CIT0001 article-title: Henipaviruses – volume: 85 start-page: 946 year: 2011 ident: 2020051111580570200_CIT0003 article-title: Pteropid bats are confirmed as the reservoir hosts of henipaviruses: a comprehensive experimental study of virus transmission publication-title: Am J Trop Med Hyg doi: 10.4269/ajtmh.2011.10-0567 – volume: 5 start-page: 24 year: 2014 ident: 2020051111580570200_CIT0043 article-title: Activation of paramyxovirus membrane fusion and virus entry publication-title: Curr Opin Virol doi: 10.1016/j.coviro.2014.01.005 – volume: 21 start-page: 328 year: 2015 ident: 2020051111580570200_CIT0014 article-title: Outbreak of henipavirus infection, Philippines, 2014 publication-title: Emerg Infect Dis doi: 10.3201/eid2102.141433 – volume: 201 start-page: 946 year: 2010 ident: 2020051111580570200_CIT0047 article-title: Escape from human monoclonal antibody neutralization affects in vitro and in vivo fitness of severe acute respiratory syndrome coronavirus publication-title: J Infect Dis doi: 10.1086/651022 – volume: 10 start-page: 237 year: 2013 ident: 2020051111580570200_CIT0035 article-title: Vaccination of ferrets with a recombinant G glycoprotein subunit vaccine provides protection against Nipah virus disease for over 12 months publication-title: Virol J doi: 10.1186/1743-422X-10-237 – volume: 359 start-page: 197 year: 2012 ident: 2020051111580570200_CIT0021 article-title: Immunization strategies against henipaviruses publication-title: Curr Top Microbiol Immunol – year: 2019 ident: 2020051111580570200_CIT0031 article-title: A potent cross-neutralizing antibody targeting the fusion glycoprotein inhibits Nipah virus and Hendra virus infection publication-title: Nat Struct Mol Biol doi: 10.1038/s41594-019-0308-9 – volume: 29 start-page: 5623 year: 2011 ident: 2020051111580570200_CIT0034 article-title: A recombinant Hendra virus G glycoprotein-based subunit vaccine protects ferrets from lethal Hendra virus challenge publication-title: Vaccine doi: 10.1016/j.vaccine.2011.06.015 – volume: 6 start-page: 30916 year: 2016 ident: 2020051111580570200_CIT0026 article-title: Pathogenic differences between Nipah virus Bangladesh and Malaysia strains in primates: implications for antibody Therapy publication-title: Sci Rep doi: 10.1038/srep30916 – start-page: 996 volume-title: Fields Virology year: 2013 ident: 2020051111580570200_CIT0037 article-title: Parainfluenza viruses – volume: 16 start-page: 120 year: 2016 ident: 2020051111580570200_CIT0004 article-title: Hendra virus ecology and transmission publication-title: Curr Opin Virol doi: 10.1016/j.coviro.2016.02.004 – volume: 790 start-page: 95 year: 2013 ident: 2020051111580570200_CIT0018 article-title: Paramyxovirus entry publication-title: Adv Exp Med Biol doi: 10.1007/978-1-4614-7651-1_6 – volume: 10 start-page: e0004775 year: 2016 ident: 2020051111580570200_CIT0032 article-title: The nature of exposure drives transmission of Nipah viruses from Malaysia and Bangladesh in ferrets publication-title: PLoS Negl Trop Dis doi: 10.1371/journal.pntd.0004775 – volume: 86 start-page: 11457 year: 2012 ident: 2020051111580570200_CIT0029 article-title: Biochemical, conformational, and immunogenic analysis of soluble trimeric forms of henipavirus fusion glycoproteins publication-title: J Virol doi: 10.1128/JVI.01318-12 – volume: 359 start-page: 153 year: 2012 ident: 2020051111580570200_CIT0002 article-title: Animal challenge models of henipavirus infection and pathogenesis publication-title: Curr Top Microbiol Immunol – volume: 514 start-page: 47 year: 2014 ident: 2020051111580570200_CIT0046 article-title: Reversion of advanced Ebola virus disease in nonhuman primates with ZMapp publication-title: Nature doi: 10.1038/nature13777 – volume: 288 start-page: 1432 year: 2000 ident: 2020051111580570200_CIT0011 article-title: Nipah virus: a recently emergent deadly paramyxovirus publication-title: Science doi: 10.1126/science.288.5470.1432 – volume: 13 start-page: 9 year: 2017 ident: 2020051111580570200_CIT0015 article-title: Global research trends of World Health Organization’s top eight emerging pathogens publication-title: Global Health doi: 10.1186/s12992-017-0233-9 – volume-title: Henipavirus gap analysis workshop report year: 2018 ident: 2020051111580570200_CIT0008 – volume: 12 start-page: 235 year: 2006 ident: 2020051111580570200_CIT0012 article-title: Nipah virus-associated encephalitis outbreak, Siliguri, India publication-title: Emerg Infect Dis doi: 10.3201/eid1202.051247 – volume: 81 start-page: 1927 year: 2000 ident: 2020051111580570200_CIT0005 article-title: Isolation of Hendra virus from pteropid bats: a natural reservoir of Hendra virus publication-title: J Gen Virol doi: 10.1099/0022-1317-81-8-1927 – volume: 80 start-page: 1972 year: 2006 ident: 2020051111580570200_CIT0042 article-title: Antibody prophylaxis and therapy against Nipah virus infection in hamsters publication-title: J Virol doi: 10.1128/JVI.80.4.1972-1978.2006 – volume: 113 start-page: 1056 year: 2016 ident: 2020051111580570200_CIT0030 article-title: Structure and stabilization of the Hendra virus F glycoprotein in its prefusion form publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.1523303113 – volume: 34 start-page: 3525 year: 2016 ident: 2020051111580570200_CIT0010 article-title: Hendra virus and Nipah virus animal vaccines publication-title: Vaccine doi: 10.1016/j.vaccine.2016.03.075 – volume: 10 start-page: 2082 year: 2004 ident: 2020051111580570200_CIT0013 article-title: Nipah virus encephalitis reemergence, Bangladesh publication-title: Emerg Infect Dis doi: 10.3201/eid1012.040701 – volume: 181 start-page: 211 year: 2009 ident: 2020051111580570200_CIT0017 article-title: Animal models of henipavirus infection: a review publication-title: Vet J doi: 10.1016/j.tvjl.2008.10.016 – volume: 102 start-page: 10652 year: 2005 ident: 2020051111580570200_CIT0019 article-title: Ephrin-B2 ligand is a functional receptor for Hendra virus and Nipah virus publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.0504887102 – volume: 80 start-page: 891 year: 2006 ident: 2020051111580570200_CIT0023 article-title: Potent neutralization of Hendra and Nipah viruses by human monoclonal antibodies publication-title: J Virol doi: 10.1128/JVI.80.2.891-899.2006 – volume: 197 start-page: 846 year: 2008 ident: 2020051111580570200_CIT0024 article-title: Exceptionally potent cross-reactive neutralization of Nipah and Hendra viruses by a human monoclonal antibody publication-title: J Infect Dis doi: 10.1086/528801 – volume: 6 start-page: 242ra82 year: 2014 ident: 2020051111580570200_CIT0027 article-title: Therapeutic treatment of Nipah virus infection in nonhuman primates with a neutralizing human monoclonal antibody publication-title: Sci Transl Med doi: 10.1126/scitranslmed.3008929 – volume: 12 start-page: e0006343 year: 2018 ident: 2020051111580570200_CIT0033 article-title: Host gene expression profiles in ferrets infected with genetically distinct henipavirus strains publication-title: PLoS Negl Trop Dis doi: 10.1371/journal.pntd.0006343 – volume: 6 start-page: 7483 year: 2015 ident: 2020051111580570200_CIT0036 article-title: The immunomodulating V and W proteins of Nipah virus determine disease course publication-title: Nat Commun doi: 10.1038/ncomms8483 – volume: 25 start-page: 166 year: 2019 ident: 2020051111580570200_CIT0007 article-title: Isolation and full-genome characterization of Nipah viruses from bats, Bangladesh publication-title: Emerg Infect Dis doi: 10.3201/eid2501.180267 – start-page: 1042 volume-title: Fields Virology year: 2013 ident: 2020051111580570200_CIT0039 article-title: Measles virus – volume: 5 start-page: e1000642 year: 2009 ident: 2020051111580570200_CIT0025 article-title: A neutralizing human monoclonal antibody protects against lethal disease in a new ferret model of acute nipah virus infection publication-title: PLoS Pathog doi: 10.1371/journal.ppat.1000642 – volume: 2 start-page: 695 year: 2004 ident: 2020051111580570200_CIT0040 article-title: Passive antibody therapy for infectious diseases publication-title: Nat Rev Microbiol doi: 10.1038/nrmicro974 – volume: 4 start-page: 145 year: 2002 ident: 2020051111580570200_CIT0006 article-title: Isolation of Nipah virus from Malaysian Island flying-foxes publication-title: Microbes Infect doi: 10.1016/S1286-4579(01)01522-2 – volume: 387 start-page: 459 year: 2009 ident: 2020051111580570200_CIT0041 article-title: Acute Hendra virus infection: analysis of the pathogenesis and passive antibody protection in the hamster model publication-title: Virology doi: 10.1016/j.virol.2009.03.001 – volume: 436 start-page: 401 year: 2005 ident: 2020051111580570200_CIT0020 article-title: EphrinB2 is the entry receptor for Nipah virus, an emergent deadly paramyxovirus publication-title: Nature doi: 10.1038/nature03838 – volume: 3 start-page: 105ra3 year: 2011 ident: 2020051111580570200_CIT0028 article-title: A neutralizing human monoclonal antibody protects African green monkeys from Hendra virus challenge publication-title: Sci Transl Med doi: 10.1126/scitranslmed.3002901 |
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Background
Nipah virus (NiV) and Hendra virus (HeV) are zoonotic paramyxoviruses that cause severe disease in both animals and humans. There are no... Nipah virus (NiV) and Hendra virus (HeV) are zoonotic paramyxoviruses that cause severe disease in both animals and humans. There are no approved vaccines or... Background Nipah virus (NiV) and Hendra virus (HeV) are zoonotic paramyxoviruses that cause severe disease in both animals and humans. There are no approved... |
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| SubjectTerms | Animals Antibodies Antibodies, Monoclonal - therapeutic use Antiviral activity Antiviral drugs Cross Reactions Epitopes Ferrets Glycoproteins Hendra Virus Henipavirus Infections - prevention & control Henipavirus Infections - therapy Henipavirus Infections - virology Humans Immunotherapy Infections Membrane fusion Monoclonal antibodies Mustela Nipah Virus Supplement Viral Fusion Proteins - immunology Zoonoses |
| Title | A Cross-Reactive Humanized Monoclonal Antibody Targeting Fusion Glycoprotein Function Protects Ferrets Against Lethal Nipah Virus and Hendra Virus Infection |
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