메뉴 건너뛰기




Volumn 2, Issue 1, 2017, Pages

Antibody therapies for the prevention and treatment of viral infections

Author keywords

[No Author keywords available]

Indexed keywords


EID: 85042287795     PISSN: None     EISSN: 20590105     Source Type: Journal    
DOI: 10.1038/s41541-017-0019-3     Document Type: Review
Times cited : (146)

References (157)
  • 2
    • 2942635256 scopus 로고    scopus 로고
    • Paul Ehrlich-in search of the magic bullet
    • Winau, F., Westphal, O., Winau, R. Paul Ehrlich-in search of the magic bullet. Microbes Infect. 6, 786-789 (2004).
    • (2004) Microbes Infect. , vol.6 , pp. 786-789
    • Winau, F.1    Westphal, O.2    Winau, R.3
  • 3
    • 33748975332 scopus 로고    scopus 로고
    • Basic principles of intravenous immunoglobulin (IVIg) treatment
    • Stangel, M., Pul, R. Basic principles of intravenous immunoglobulin (IVIg) treatment. J. Neurol. 253, V18-24 (2006).
    • (2006) J. Neurol. , vol.253 , pp. V18-24
    • Stangel, M.1    Pul, R.2
  • 4
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Kohler, G., Milstein, C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 256, 495-497 (1975).
    • (1975) Nature , vol.256 , pp. 495-497
    • Kohler, G.1    Milstein, C.2
  • 5
    • 58049198443 scopus 로고    scopus 로고
    • Heterosubtypic neutralizing monoclonal antibodies cross-protective against H5N1 and H1N1 recovered from human IgM+memory B cells
    • Throsby, M., et al. Heterosubtypic neutralizing monoclonal antibodies cross-protective against H5N1 and H1N1 recovered from human IgM+memory B cells. PLoS ONE 3, e3942 (2008).
    • (2008) PLoS ONE , vol.3 , pp. e3942
    • Throsby, M.1
  • 6
    • 84879167987 scopus 로고    scopus 로고
    • Rapid generation of human-like neutralizing monoclonal antibodies in urgent preparedness for influenza pandemics and virulent infectious diseases
    • Meng, W., et al. Rapid generation of human-like neutralizing monoclonal antibodies in urgent preparedness for influenza pandemics and virulent infectious diseases. PLoS ONE 8, e66276 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e66276
    • Meng, W.1
  • 7
    • 3042647616 scopus 로고    scopus 로고
    • Anchored periplasmic expression, a versatile technology for the isolation of high-affinity antibodies from Escherichia coli-expressed libraries
    • Harvey, B. R., et al. Anchored periplasmic expression, a versatile technology for the isolation of high-affinity antibodies from Escherichia coli-expressed libraries. Proc. Natl Acad. Sci. U.S.A. 101, 9193-9198 (2004).
    • (2004) Proc. Natl Acad. Sci. U.S.A. , vol.101 , pp. 9193-9198
    • Harvey, B.R.1
  • 8
    • 33947155314 scopus 로고    scopus 로고
    • Antigen selection from an HIV-1 immune antibody library displayed on yeast yields many novel antibodies compared to selection from the same library displayed on phage
    • Bowley, D. R., Labrijn, A. F., Zwick, M. B., Burton, D. R. Antigen selection from an HIV-1 immune antibody library displayed on yeast yields many novel antibodies compared to selection from the same library displayed on phage. Protein Eng. Des. Sel. 20, 81-90 (2007).
    • (2007) Protein Eng. Des. Sel. , vol.20 , pp. 81-90
    • Bowley, D.R.1    Labrijn, A.F.2    Zwick, M.B.3    Burton, D.R.4
  • 10
    • 84884991510 scopus 로고    scopus 로고
    • Isolation of human monoclonal antibodies from peripheral blood B cells
    • Huang, J., et al. Isolation of human monoclonal antibodies from peripheral blood B cells. Nat. Protoc. 8, 1907-1915 (2013).
    • (2013) Nat. Protoc. , vol.8 , pp. 1907-1915
    • Huang, J.1
  • 11
    • 70349887757 scopus 로고    scopus 로고
    • Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target
    • Walker, L. M., et al. Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target. Science 326, 285-289 (2009).
    • (2009) Science , vol.326 , pp. 285-289
    • Walker, L.M.1
  • 12
    • 63849131879 scopus 로고    scopus 로고
    • Broad diversity of neutralizing antibodies isolated from memory B cells in HIV-infected individuals
    • Scheid, J. F., et al. Broad diversity of neutralizing antibodies isolated from memory B cells in HIV-infected individuals. Nature 458, 636-640 (2009).
    • (2009) Nature , vol.458 , pp. 636-640
    • Scheid, J.F.1
  • 13
    • 4043154176 scopus 로고    scopus 로고
    • An efficient method to make human monoclonal antibodies from memory B cells: Potent neutralization of SARS coronavirus
    • Traggiai, E., et al. An efficient method to make human monoclonal antibodies from memory B cells: Potent neutralization of SARS coronavirus. Nat. Med. 10, 871-875 (2004).
    • (2004) Nat. Med. , vol.10 , pp. 871-875
    • Traggiai, E.1
  • 14
    • 77956688921 scopus 로고    scopus 로고
    • Monoclonal antibodies isolated without screening by analyzing the variable-gene repertoire of plasma cells
    • Reddy, S. T., et al. Monoclonal antibodies isolated without screening by analyzing the variable-gene repertoire of plasma cells. Nat. Biotechnol. 28, 965-969 (2010).
    • (2010) Nat. Biotechnol. , vol.28 , pp. 965-969
    • Reddy, S.T.1
  • 15
    • 44449118948 scopus 로고    scopus 로고
    • Rapid cloning of high-affinity human monoclonal antibodies against influenza virus
    • Wrammert, J., et al. Rapid cloning of high-affinity human monoclonal antibodies against influenza virus. Nature 453, 667-671 (2008).
    • (2008) Nature , vol.453 , pp. 667-671
    • Wrammert, J.1
  • 16
    • 84983592003 scopus 로고    scopus 로고
    • Efficient generation of monoclonal antibodies from single rhesus macaque antibody secreting cells
    • Meng, W., et al. Efficient generation of monoclonal antibodies from single rhesus macaque antibody secreting cells. MAbs 7, 707-718 (2015).
    • (2015) MAbs , vol.7 , pp. 707-718
    • Meng, W.1
  • 17
    • 84860381828 scopus 로고    scopus 로고
    • A proteomics approach for the identification and cloning of monoclonal antibodies from serum
    • doi:nbt.2167 [pii]
    • Cheung, W. C., et al. A proteomics approach for the identification and cloning of monoclonal antibodies from serum. Nat. Biotechnol., doi:nbt.2167 [pii], 10.1038/nbt.2167 (2012).
    • (2012) Nat. Biotechnol
    • Cheung, W.C.1
  • 18
    • 84874223925 scopus 로고    scopus 로고
    • Molecular deconvolution of the monoclonal antibodies that comprise the polyclonal serum response
    • Wine, Y., et al. Molecular deconvolution of the monoclonal antibodies that comprise the polyclonal serum response. Proc. Natl Acad. Sci. U.S.A. 110, 2993-2998 (2013).
    • (2013) Proc. Natl Acad. Sci. U.S.A. , vol.110 , pp. 2993-2998
    • Wine, Y.1
  • 19
    • 84959350663 scopus 로고    scopus 로고
    • Ultra-high-throughput sequencing of the immune receptor repertoire from millions of lymphocytes
    • McDaniel, J. R., DeKosky, B. J., Tanno, H., Ellington, A. D., Georgiou, G. Ultra-high-throughput sequencing of the immune receptor repertoire from millions of lymphocytes. Nat. Protoc. 11, 429-442 (2016).
    • (2016) Nat. Protoc. , vol.11 , pp. 429-442
    • McDaniel, J.R.1    DeKosky, B.J.2    Tanno, H.3    Ellington, A.D.4    Georgiou, G.5
  • 20
    • 84925284996 scopus 로고    scopus 로고
    • In-depth determination and analysis of the human paired heavy- A nd light-chain antibody repertoire
    • DeKosky, B. J., et al. In-depth determination and analysis of the human paired heavy- A nd light-chain antibody repertoire. Nat. Med. 21, 86-91 (2015).
    • (2015) Nat. Med. , vol.21 , pp. 86-91
    • DeKosky, B.J.1
  • 21
    • 26844448487 scopus 로고    scopus 로고
    • A human monoclonal antibody neutralizes diverse HIV-1 isolates by binding a critical gp41 epitope
    • Miller, M. D., et al. A human monoclonal antibody neutralizes diverse HIV-1 isolates by binding a critical gp41 epitope. Proc. Natl Acad. Sci. U.S.A. 102, 14759-14764 (2005).
    • (2005) Proc. Natl Acad. Sci. U.S.A. , vol.102 , pp. 14759-14764
    • Miller, M.D.1
  • 22
    • 84958825022 scopus 로고    scopus 로고
    • Efficient methods to isolate human monoclonal antibodies from memory b cells and plasma cells
    • Corti, D., Lanzavecchia, A. Efficient methods to isolate human monoclonal antibodies from memory b cells and plasma cells. Microbiol. Spectr. 2, doi: 10.1128/microbiolspec.AID-0018-2014 (2014).
    • (2014) Microbiol. Spectr. , vol.2
    • Corti, D.1    Lanzavecchia, A.2
  • 23
    • 85006488816 scopus 로고    scopus 로고
    • Molecular determinants of human neutralizing antibodies isolated from a patient infected with Zika virus
    • Wang, Q., et al. Molecular determinants of human neutralizing antibodies isolated from a patient infected with Zika virus. Sci, Transl. Med. 8, 369ra179, doi: 10.1126/scitranslmed.aai8336 (2016).
    • (2016) Sci. Transl. Med. , vol.8 , pp. 369ra179
    • Wang, Q.1
  • 24
    • 85014096226 scopus 로고    scopus 로고
    • Rapid profiling of RSV antibody repertoires from the memory B cells of naturally infected adult donors
    • Gilman, M. S. A., et al. Rapid profiling of RSV antibody repertoires from the memory B cells of naturally infected adult donors. Sci. Immunol. 1, doi: 10.1126/sciimmunol.aaj1879 (2016).
    • (2016) Sci. Immunol. , vol.1
    • Gilman, M.S.A.1
  • 25
    • 84908329318 scopus 로고    scopus 로고
    • Characteristics of memory B cells elicited by a highly efficacious HPV vaccine in subjects with no pre-existing immunity
    • Scherer, E. M., et al. Characteristics of memory B cells elicited by a highly efficacious HPV vaccine in subjects with no pre-existing immunity. PLoS Pathog. 10, e1004461 (2014).
    • (2014) PLoS Pathog. , vol.10 , pp. e1004461
    • Scherer, E.M.1
  • 26
    • 84898652113 scopus 로고    scopus 로고
    • Single-cell and deep sequencing of IgG-switched macaque B cells reveal a diverse Ig repertoire following immunization
    • Sundling, C., et al. Single-cell and deep sequencing of IgG-switched macaque B cells reveal a diverse Ig repertoire following immunization. J. Immunol. 192, 3637-3644 (2014).
    • (2014) J. Immunol. , vol.192 , pp. 3637-3644
    • Sundling, C.1
  • 27
    • 0025190715 scopus 로고
    • Clonal analysis of a human antibody response. Quantitation of precursors of antibody-producing cells and generation and characterization of monoclonal IgM IgG, and IgA to rabies virus
    • Ueki, Y., et al. Clonal analysis of a human antibody response. Quantitation of precursors of antibody-producing cells and generation and characterization of monoclonal IgM, IgG, and IgA to rabies virus. J. Exp. Med. 171, 19-34 (1990).
    • (1990) J. Exp. Med. , vol.171 , pp. 19-34
    • Ueki, Y.1
  • 28
    • 0037073930 scopus 로고    scopus 로고
    • Maintenance of serological memory by polyclonal activation of human memory B cells
    • Bernasconi, N. L., Traggiai, E., Lanzavecchia, A. Maintenance of serological memory by polyclonal activation of human memory B cells. Science 298, 2199-2202 (2002).
    • (2002) Science , vol.298 , pp. 2199-2202
    • Bernasconi, N.L.1    Traggiai, E.2    Lanzavecchia, A.3
  • 29
    • 80051670323 scopus 로고    scopus 로고
    • A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins
    • Corti, D., et al. A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins. Science 333, 850-856 (2011).
    • (2011) Science , vol.333 , pp. 850-856
    • Corti, D.1
  • 30
    • 63849240274 scopus 로고    scopus 로고
    • Rapid generation of fully human monoclonal antibodies specific to a vaccinating antigen
    • Smith, K., et al. Rapid generation of fully human monoclonal antibodies specific to a vaccinating antigen. Nat. Protoc. 4, 372-384 (2009).
    • (2009) Nat. Protoc. , vol.4 , pp. 372-384
    • Smith, K.1
  • 31
    • 84857963464 scopus 로고    scopus 로고
    • Rapid and massive virus-specific plasmablast responses during acute dengue virus infection in humans
    • Wrammert, J., et al. Rapid and massive virus-specific plasmablast responses during acute dengue virus infection in humans. J. Virol. 86, 2911-2918 (2012).
    • (2012) J. Virol. , vol.86 , pp. 2911-2918
    • Wrammert, J.1
  • 32
    • 84880427552 scopus 로고    scopus 로고
    • An in vivo human-plasmablast enrichment technique allows rapid identification of therapeutic influenza A antibodies
    • Nakamura, G., et al. An in vivo human-plasmablast enrichment technique allows rapid identification of therapeutic influenza A antibodies. Cell Host Microbe. 14, 93-103 (2013).
    • (2013) Cell Host Microbe. , vol.14 , pp. 93-103
    • Nakamura, G.1
  • 33
    • 84922947115 scopus 로고    scopus 로고
    • A new class of highly potent, broadly neutralizing antibodies isolated from viremic patients infected with dengue virus
    • Dejnirattisai, W., et al. A new class of highly potent, broadly neutralizing antibodies isolated from viremic patients infected with dengue virus. Nat. Immunol. 16, 170-177 (2015).
    • (2015) Nat. Immunol. , vol.16 , pp. 170-177
    • Dejnirattisai, W.1
  • 34
    • 78651488739 scopus 로고    scopus 로고
    • Broadly cross-reactive antibodies dominate the human B cell response against 2009 pandemic H1N1 influenza virus infection
    • Wrammert, J., et al. Broadly cross-reactive antibodies dominate the human B cell response against 2009 pandemic H1N1 influenza virus infection. J. Exp. Med. 208, 181-193 (2011).
    • (2011) J. Exp. Med. , vol.208 , pp. 181-193
    • Wrammert, J.1
  • 35
    • 84867481204 scopus 로고    scopus 로고
    • Isolation of antibody V(D) J sequences from single cell sorted rhesus macaque B cells
    • Sundling, C., Phad, G., Douagi, I., Navis, M., Karlsson Hedestam, G. B. Isolation of antibody V(D)J sequences from single cell sorted rhesus macaque B cells. J. Immunol. Methods 386, 85-93 (2012).
    • (2012) J. Immunol. Methods , vol.386 , pp. 85-93
    • Sundling, C.1    Phad, G.2    Douagi, I.3    Navis, M.4    Karlsson Hedestam, G.B.5
  • 36
    • 84869217139 scopus 로고    scopus 로고
    • Dynamics of memory B-cell populations in blood, lymph nodes, and bone marrow during antiretroviral therapy and envelope boosting in simian immunodeficiency virus SIVmac251-infected rhesus macaques
    • Demberg, T., et al. Dynamics of memory B-cell populations in blood, lymph nodes, and bone marrow during antiretroviral therapy and envelope boosting in simian immunodeficiency virus SIVmac251-infected rhesus macaques. J. Virol. 86, 12591-12604 (2012).
    • (2012) J. Virol. , vol.86 , pp. 12591-12604
    • Demberg, T.1
  • 37
    • 69949151874 scopus 로고    scopus 로고
    • A rapid and efficient single-cell manipulation method for screening antigen-specific antibody-secreting cells from human peripheral blood
    • Jin, A., et al. A rapid and efficient single-cell manipulation method for screening antigen-specific antibody-secreting cells from human peripheral blood. Nat. Med. 15, 1088-1092 (2009).
    • (2009) Nat. Med. , vol.15 , pp. 1088-1092
    • Jin, A.1
  • 38
    • 84869438827 scopus 로고    scopus 로고
    • Proteomics-directed cloning of circulating antiviral human monoclonal antibodies
    • Sato, S., et al. Proteomics-directed cloning of circulating antiviral human monoclonal antibodies. Nat. Biotechnol. 30, 1039-1043 (2012).
    • (2012) Nat. Biotechnol. , vol.30 , pp. 1039-1043
    • Sato, S.1
  • 39
    • 84901253129 scopus 로고    scopus 로고
    • Proteomic identification of monoclonal antibodies from serum
    • Boutz, D. R., et al. Proteomic identification of monoclonal antibodies from serum. Anal. Chem. 86, 4758-4766 (2014).
    • (2014) Anal. Chem. , vol.86 , pp. 4758-4766
    • Boutz, D.R.1
  • 40
    • 80052942203 scopus 로고    scopus 로고
    • Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing
    • Wu, X., et al. Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing. Science 333, 1593-1602 (2011).
    • (2011) Science , vol.333 , pp. 1593-1602
    • Wu, X.1
  • 41
    • 84876272159 scopus 로고    scopus 로고
    • Mining the antibodyome for HIV-1-neutralizing antibodies with next-generation sequencing and phylogenetic pairing of heavy/light chains
    • Zhu, J., et al. Mining the antibodyome for HIV-1-neutralizing antibodies with next-generation sequencing and phylogenetic pairing of heavy/light chains. Proc. Natl Acad. Sci. USA, doi: 10.1073/pnas.1219320110 (2013).
    • (2013) Proc. Natl Acad. Sci. USA
    • Zhu, J.1
  • 42
    • 84873605796 scopus 로고    scopus 로고
    • High-throughput sequencing of the paired human immunoglobulin heavy and light chain repertoire
    • Dekosky, B. J., et al. High-throughput sequencing of the paired human immunoglobulin heavy and light chain repertoire. Nat. Biotechnol., doi: 10.1038/nbt.2492 (2013).
    • (2013) Nat. Biotechnol.
    • Dekosky, B.J.1
  • 43
    • 84898545160 scopus 로고    scopus 로고
    • Progress on pursuit of human cytomegalovirus vaccines for prevention of congenital infection and disease
    • Fu, T. M., An, Z., Wang, D. Progress on pursuit of human cytomegalovirus vaccines for prevention of congenital infection and disease. Vaccine 32, 2525-2533 (2014).
    • (2014) Vaccine , vol.32 , pp. 2525-2533
    • Fu, T.M.1    An, Z.2    Wang, D.3
  • 44
    • 84994037030 scopus 로고    scopus 로고
    • A replication-defective human cytomegalovirus vaccine for prevention of congenital infection
    • Wang, D., et al. A replication-defective human cytomegalovirus vaccine for prevention of congenital infection. Sci. Transl. Med. 8, 362ra145 (2016).
    • (2016) Sci. Transl. Med. , vol.8 , pp. 145-362
    • Wang, D.1
  • 45
    • 84887907189 scopus 로고    scopus 로고
    • Resistance of human cytomegalovirus to ganciclovir/valganciclovir: A comprehensive review of putative resistance pathways
    • Komatsu, T. E., Pikis, A., Naeger, L. K., Harrington, P. R. Resistance of human cytomegalovirus to ganciclovir/valganciclovir: A comprehensive review of putative resistance pathways. Antiviral Res. 101, 12-25 (2014).
    • (2014) Antiviral Res. , vol.101 , pp. 12-25
    • Komatsu, T.E.1    Pikis, A.2    Naeger, L.K.3    Harrington, P.R.4
  • 46
    • 84992745889 scopus 로고    scopus 로고
    • Detection of low frequency multi-drug resistance and novel putative maribavir resistance in immunocompromised pediatric patients with cytomegalovirus
    • Houldcroft, C. J., et al. Detection of low frequency multi-drug resistance and novel putative maribavir resistance in immunocompromised pediatric patients with cytomegalovirus. Front. Microbiol. 7, 1317 (2016).
    • (2016) Front. Microbiol. , vol.7 , pp. 1317
    • Houldcroft, C.J.1
  • 47
    • 84897551308 scopus 로고    scopus 로고
    • A randomized trial of hyperimmune globulin to prevent congenital cytomegalovirus
    • Revello, M. G., et al. A randomized trial of hyperimmune globulin to prevent congenital cytomegalovirus. N. Engl. J. Med. 370, 1316-1326 (2014).
    • (2014) N. Engl. J. Med. , vol.370 , pp. 1316-1326
    • Revello, M.G.1
  • 48
    • 84964875188 scopus 로고    scopus 로고
    • A first-in-human study to assess the safety and pharmacokinetics of monoclonal antibodies against human cytomegalovirus in healthy volunteers
    • Dole, K., et al. A first-in-human study to assess the safety and pharmacokinetics of monoclonal antibodies against human cytomegalovirus in healthy volunteers. Antimicrob. Agents Chemother., doi: 10.1128/AAC.02698-15 (2016).
    • (2016) Antimicrob. Agents Chemother.
    • Dole, K.1
  • 49
    • 84939804512 scopus 로고    scopus 로고
    • Phase 1 randomized, double-blind, placebo-controlled study of RG7667, an anticytomegalovirus combination monoclonal antibody therapy, in healthy adults
    • Ishida, J. H., et al. Phase 1 randomized, double-blind, placebo-controlled study of RG7667, an anticytomegalovirus combination monoclonal antibody therapy, in healthy adults. Antimicrob. Agents Chemother. 59, 4919-4929 (2015).
    • (2015) Antimicrob. Agents Chemother. , vol.59 , pp. 4919-4929
    • Ishida, J.H.1
  • 50
    • 84890850632 scopus 로고    scopus 로고
    • Pentameric complex of viral glycoprotein H is the primary target for potent neutralization by a human cytomegalovirus vaccine
    • Freed, D. C., et al. Pentameric complex of viral glycoprotein H is the primary target for potent neutralization by a human cytomegalovirus vaccine. Proc. Natl Acad. Sci. U.S.A. 110, E4997-5005 (2013).
    • (2013) Proc. Natl Acad. Sci. U.S.A. , vol.110 , pp. E4997-5005
    • Freed, D.C.1
  • 51
    • 84939267590 scopus 로고    scopus 로고
    • Human antibody technology and the development of antibodies against cytomegalovirus
    • Ohlin, M., Soderberg-Naucler, C. Human antibody technology and the development of antibodies against cytomegalovirus. Mol. Immunol., doi: 10.1016/j.molimm.2015.02.026 (2015).
    • (2015) Mol. Immunol.
    • Ohlin, M.1    Soderberg-Naucler, C.2
  • 52
    • 73849089855 scopus 로고    scopus 로고
    • Isolation of human monoclonal antibodies that potently neutralize human cytomegalovirus infection by targeting different epitopes on the gH/gL/UL128-131A complex
    • Macagno, A., et al. Isolation of human monoclonal antibodies that potently neutralize human cytomegalovirus infection by targeting different epitopes on the gH/gL/UL128-131A complex. J. Virol. 84, 1005-1013 (2010).
    • (2010) J. Virol. , vol.84 , pp. 1005-1013
    • MacAgno, A.1
  • 53
    • 84979581127 scopus 로고    scopus 로고
    • In vitro characterization of human cytomegalovirus-targeting therapeutic monoclonal antibodies LJP538 and LJP539
    • Patel, H. D., et al. In vitro characterization of human cytomegalovirus-targeting therapeutic monoclonal antibodies LJP538 and LJP539. Antimicrob. Agents Chemother. 60, 4961-4971 (2016).
    • (2016) Antimicrob. Agents Chemother. , vol.60 , pp. 4961-4971
    • Patel, H.D.1
  • 55
    • 84896516865 scopus 로고    scopus 로고
    • In vitro affinity maturation of a natural human antibody overcomes a barrier to in vivo affinity maturation
    • Li, B., et al. In vitro affinity maturation of a natural human antibody overcomes a barrier to in vivo affinity maturation. MAbs 6, 437-445 (2014).
    • (2014) MAbs , vol.6 , pp. 437-445
    • Li, B.1
  • 56
    • 7444237579 scopus 로고    scopus 로고
    • A phase II, double-masked, randomized, placebo-controlled evaluation of a human monoclonal anti-Cytomegalovirus antibody (MSL-109) in combination with standard therapy versus standard therapy alone in the treatment of AIDS patients with Cytomegalovirus retinitis
    • Borucki, M. J., et al. A phase II, double-masked, randomized, placebo-controlled evaluation of a human monoclonal anti-Cytomegalovirus antibody (MSL-109) in combination with standard therapy versus standard therapy alone in the treatment of AIDS patients with Cytomegalovirus retinitis. Antiviral Res. 64, 103-111 (2004).
    • (2004) Antiviral Res. , vol.64 , pp. 103-111
    • Borucki, M.J.1
  • 57
    • 80053019483 scopus 로고    scopus 로고
    • Human cytomegalovirus escapes a naturally occurring neutralizing antibody by incorporating it into assembling virions
    • Manley, K., et al. Human cytomegalovirus escapes a naturally occurring neutralizing antibody by incorporating it into assembling virions. Cell Host Microbe 10, 197-209 (2011).
    • (2011) Cell Host Microbe , vol.10 , pp. 197-209
    • Manley, K.1
  • 58
    • 85042275639 scopus 로고    scopus 로고
    • Phase 2 randomized, double-blind, placebo-controlled trial of RG7667, a combination monoclonal antibody, for prevention of cytomegalovirus infection in high-risk kidney transplant recipients
    • Ishida, J. H., et al. Phase 2 randomized, double-blind, placebo-controlled trial of RG7667, a combination monoclonal antibody, for prevention of cytomegalovirus infection in high-risk kidney transplant recipients. Antimicrob. Agents Chemother. (2016).
    • (2016) Antimicrob. Agents Chemother
    • Ishida, J.H.1
  • 59
    • 85008249238 scopus 로고    scopus 로고
    • The pharmacological management of severe influenza infection-'existing and emerging therapies
    • Mc Mahon, A., Martin-Loeches, I. The pharmacological management of severe influenza infection-'existing and emerging therapies'. Expert Rev. Clin. Pharmacol. 10, 81-95 (2017).
    • (2017) Expert Rev. Clin. Pharmacol. , vol.10 , pp. 81-95
    • Mc Mahon, A.1    Martin-Loeches, I.2
  • 60
    • 84922225958 scopus 로고    scopus 로고
    • Rapid development of broadly influenza neutralizing antibodies through redundant mutations
    • Pappas, L., et al. Rapid development of broadly influenza neutralizing antibodies through redundant mutations. Nature 516, 418-422 (2014).
    • (2014) Nature , vol.516 , pp. 418-422
    • Pappas, L.1
  • 61
    • 84959349464 scopus 로고    scopus 로고
    • Novel universal influenza virus vaccine approaches
    • Krammer, F. Novel universal influenza virus vaccine approaches. Curr. Opin. Virol. 17, 95-103 (2016).
    • (2016) Curr. Opin. Virol. , vol.17 , pp. 95-103
    • Krammer, F.1
  • 62
    • 84966460100 scopus 로고    scopus 로고
    • Preclinical pharmacokinetics of MHAA4549A, a human monoclonal antibody to influenza A virus, and the prediction of its efficacious clinical dose for the treatment of patients hospitalized with influenza A
    • Gupta, P., et al. Preclinical pharmacokinetics of MHAA4549A, a human monoclonal antibody to influenza A virus, and the prediction of its efficacious clinical dose for the treatment of patients hospitalized with influenza A. MAbs 8, 991-997 (2016).
    • (2016) MAbs , vol.8 , pp. 991-997
    • Gupta, P.1
  • 63
    • 84983490282 scopus 로고    scopus 로고
    • Two phase 1, randomized, double-blind, placebo-controlled, single-ascending-dose studies to investigate the safety, tolerability, and pharmacokinetics of an anti-influenza A virus monoclonal antibody, MHAA4549A, in healthy volunteers
    • Lim, J. J., et al. Two phase 1, randomized, double-blind, placebo-controlled, single-ascending-dose studies to investigate the safety, tolerability, and pharmacokinetics of an anti-influenza A virus monoclonal antibody, MHAA4549A, in healthy volunteers. Antimicrob. Agents Chemother. 60, 5437-5444 (2016).
    • (2016) Antimicrob. Agents Chemother. , vol.60 , pp. 5437-5444
    • Lim, J.J.1
  • 66
    • 85042306439 scopus 로고    scopus 로고
    • Scientists' elusive goal: Reproducing study resutls
    • Naik, G. Scientists' elusive goal: Reproducing study resutls. (Wall Street Journal, 2015).
    • (2015) Wall Street Journal
    • Naik, G.1
  • 67
    • 84963773526 scopus 로고    scopus 로고
    • The hemagglutinin stem-binding monoclonal antibody VIS410 controls influenza virus-induced acute respiratory distress syndrome
    • Baranovich, T., et al. The hemagglutinin stem-binding monoclonal antibody VIS410 controls influenza virus-induced acute respiratory distress syndrome. Antimicrob. Agents Chemother. 60, 2118-2131 (2016).
    • (2016) Antimicrob. Agents Chemother. , vol.60 , pp. 2118-2131
    • Baranovich, T.1
  • 68
    • 84959241759 scopus 로고    scopus 로고
    • Safety and upper respiratory pharmacokinetics of the hemagglutinin stalk-binding antibody VIS410 support treatment and prophylaxis based on population modeling of seasonal influenza A outbreaks
    • Wollacott, A. M., et al. Safety and upper respiratory pharmacokinetics of the hemagglutinin stalk-binding antibody VIS410 support treatment and prophylaxis based on population modeling of seasonal influenza A outbreaks. EBioMedicine 5, 147-155, doi: 10.1016/j.ebiom.2016.02.021 (2016).
    • (2016) EBioMedicine , vol.5 , pp. 147-155
    • Wollacott, A.M.1
  • 70
    • 64849114224 scopus 로고    scopus 로고
    • Antibody recognition of a highly conserved influenza virus epitope
    • Ekiert, D. C., et al. Antibody recognition of a highly conserved influenza virus epitope. Science 324, 246-251 (2009).
    • (2009) Science , vol.324 , pp. 246-251
    • Ekiert, D.C.1
  • 72
    • 80051635697 scopus 로고    scopus 로고
    • A highly conserved neutralizing epitope on group 2 influenza A viruses
    • Ekiert, D. C., et al. A highly conserved neutralizing epitope on group 2 influenza A viruses. Science 333, 843-850 (2011).
    • (2011) Science , vol.333 , pp. 843-850
    • Ekiert, D.C.1
  • 74
    • 84901024170 scopus 로고    scopus 로고
    • Broadly neutralizing influenza hemagglutinin stem-specific antibody CR8020 targets residues that are prone to escape due to host selection pressure
    • Tharakaraman, K., Subramanian, V., Cain, D., Sasisekharan, V., Sasisekharan, R. Broadly neutralizing influenza hemagglutinin stem-specific antibody CR8020 targets residues that are prone to escape due to host selection pressure. Cell Host Microbe 15, 644-651 (2014).
    • (2014) Cell Host Microbe , vol.15 , pp. 644-651
    • Tharakaraman, K.1    Subramanian, V.2    Cain, D.3    Sasisekharan, V.4    Sasisekharan, R.5
  • 75
    • 77955434077 scopus 로고    scopus 로고
    • Human antibodies reveal a protective epitope that is highly conserved among human and nonhuman influenza A viruses
    • Grandea, A. G. 3rd, et al. Human antibodies reveal a protective epitope that is highly conserved among human and nonhuman influenza A viruses. Proc. Natl Acad. Sci. U.S.A. 107, 12658-12663 (2010).
    • (2010) Proc. Natl Acad. Sci. U.S.A. , vol.107 , pp. 12658-12663
    • Grandea, A.G.1
  • 76
    • 84927732590 scopus 로고    scopus 로고
    • Efficacy and safety of treatment with an anti-m2e monoclonal antibody in experimental human influenza
    • Ramos, E. L., et al. Efficacy and safety of treatment with an anti-m2e monoclonal antibody in experimental human influenza. J. Infect. Dis. 211, 1038-1044 (2015).
    • (2015) J. Infect. Dis. , vol.211 , pp. 1038-1044
    • Ramos, E.L.1
  • 77
    • 84970951351 scopus 로고    scopus 로고
    • Harnessing the protective potential of HIV-1 neutralizing antibodies
    • Smith, S. A., Derdeyn, C. A. Harnessing the protective potential of HIV-1 neutralizing antibodies. F1000Research 5, doi: 10.12688/f1000research.7254.1 (2016).
    • (2016) F1000Research , pp. 5
    • Smith, S.A.1    Derdeyn, C.A.2
  • 78
    • 84883796903 scopus 로고    scopus 로고
    • Antibodies in HIV-1 vaccine development and therapy
    • Klein, F., et al. Antibodies in HIV-1 vaccine development and therapy. Science 341, 1199-1204 (2013).
    • (2013) Science , vol.341 , pp. 1199-1204
    • Klein, F.1
  • 80
    • 85008440477 scopus 로고    scopus 로고
    • Progress toward active or passive HIV-1 vaccination
    • Escolano, A., Dosenovic, P., Nussenzweig, M. C. Progress toward active or passive HIV-1 vaccination. J. Exp. Med. doi: 10.1084/jem.20161765 (2016).
    • (2016) J. Exp. Med.
    • Escolano, A.1    Dosenovic, P.2    Nussenzweig, M.C.3
  • 82
    • 36849087921 scopus 로고    scopus 로고
    • The growth and potential of human antiviral monoclonal antibody therapeutics
    • Marasco, W. A., Sui, J. The growth and potential of human antiviral monoclonal antibody therapeutics. Nat. Biotechnol. 25, 1421-1434 (2007).
    • (2007) Nat. Biotechnol. , vol.25 , pp. 1421-1434
    • Marasco, W.A.1    Sui, J.2
  • 83
    • 77954943648 scopus 로고    scopus 로고
    • Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01
    • Zhou, T., et al. Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01. Science 329, 811-817 (2010).
    • (2010) Science , vol.329 , pp. 811-817
    • Zhou, T.1
  • 84
    • 84962253716 scopus 로고    scopus 로고
    • Structural basis for germline antibody recognition of HIV-1 immunogens
    • Scharf, L., et al. Structural basis for germline antibody recognition of HIV-1 immunogens. Elife 5, doi: 10.7554/eLife.13783 (2016).
    • (2016) Elife , pp. 5
    • Scharf, L.1
  • 85
    • 84946480939 scopus 로고    scopus 로고
    • Safety, pharmacokinetics and neutralization of the broadly neutralizing HIV-1 human monoclonal antibody VRC01 in healthy adults
    • Ledgerwood, J. E., et al. Safety, pharmacokinetics and neutralization of the broadly neutralizing HIV-1 human monoclonal antibody VRC01 in healthy adults. Clin. Exp. Immunol. 182, 289-301 (2015).
    • (2015) Clin. Exp. Immunol. , vol.182 , pp. 289-301
    • Ledgerwood, J.E.1
  • 86
    • 84997817411 scopus 로고    scopus 로고
    • Effect of HIV antibody VRC01 on viral rebound after treatment interruption
    • Bar, K. J., et al. Effect of HIV antibody VRC01 on viral rebound after treatment interruption. N. Engl. J. Med. 375, 2037-2050 (2016).
    • (2016) N. Engl. J. Med. , vol.375 , pp. 2037-2050
    • Bar, K.J.1
  • 90
    • 80052925616 scopus 로고    scopus 로고
    • Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding
    • Scheid, J. F., et al. Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding. Science 333, 1633-1637 (2011).
    • (2011) Science , vol.333 , pp. 1633-1637
    • Scheid, J.F.1
  • 91
    • 84887627657 scopus 로고    scopus 로고
    • Antibody-mediated immunotherapy of macaques chronically infected with SHIV suppresses viraemia
    • Shingai, M., et al. Antibody-mediated immunotherapy of macaques chronically infected with SHIV suppresses viraemia. Nature 503, 277-280 (2013).
    • (2013) Nature , vol.503 , pp. 277-280
    • Shingai, M.1
  • 92
    • 84928405730 scopus 로고    scopus 로고
    • Viraemia suppressed in HIV-1-infected humans by broadly neutralizing antibody 3BNC117
    • Caskey, M., et al. Viraemia suppressed in HIV-1-infected humans by broadly neutralizing antibody 3BNC117. Nature 522, 487-491 (2015).
    • (2015) Nature , vol.522 , pp. 487-491
    • Caskey, M.1
  • 93
    • 84976406858 scopus 로고    scopus 로고
    • HIV-1 antibody 3BNC117 suppresses viral rebound in humans during treatment interruption
    • Scheid, J. F., et al. HIV-1 antibody 3BNC117 suppresses viral rebound in humans during treatment interruption. Nature 535, 556-560 (2016).
    • (2016) Nature , vol.535 , pp. 556-560
    • Scheid, J.F.1
  • 94
    • 84966341056 scopus 로고    scopus 로고
    • HIV-1 therapy with monoclonal antibody 3BNC117 elicits host immune responses against HIV-1
    • Schoofs, T., et al. HIV-1 therapy with monoclonal antibody 3BNC117 elicits host immune responses against HIV-1. Science 352, 997-1001 (2016).
    • (2016) Science , vol.352 , pp. 997-1001
    • Schoofs, T.1
  • 98
    • 33749517200 scopus 로고    scopus 로고
    • Potent antiviral synergy between monoclonal antibody and small-molecule CCR5 inhibitors of human immunodeficiency virus type 1
    • Murga, J. D., Franti, M., Pevear, D. C., Maddon, P. J., Olson, W. C. Potent antiviral synergy between monoclonal antibody and small-molecule CCR5 inhibitors of human immunodeficiency virus type 1. Antimicrob. Agents Chemother. 50, 3289-3296 (2006).
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 3289-3296
    • Murga, J.D.1    Franti, M.2    Pevear, D.C.3    Maddon, P.J.4    Olson, W.C.5
  • 99
    • 77957349209 scopus 로고    scopus 로고
    • Phase 2a study of the CCR5 monoclonal antibody PRO 140 administered intravenously to HIV-infected adults
    • Jacobson, J. M., et al. Phase 2a study of the CCR5 monoclonal antibody PRO 140 administered intravenously to HIV-infected adults. Antimicrob. Agents Chemother. 54, 4137-4142 (2010).
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 4137-4142
    • Jacobson, J.M.1
  • 100
    • 84874660180 scopus 로고    scopus 로고
    • HIV-1 entry inhibitors: Recent development and clinical use
    • Henrich, T. J., Kuritzkes, D. R. HIV-1 entry inhibitors: Recent development and clinical use. Curr. Opin. Virol. 3, 51-57 (2013).
    • (2013) Curr. Opin. Virol. , vol.3 , pp. 51-57
    • Henrich, T.J.1    Kuritzkes, D.R.2
  • 101
    • 84882404868 scopus 로고    scopus 로고
    • Bispecific antibodies directed to CD4 domain 2 and HIV envelope exhibit exceptional breadth and picomolar potency against HIV-1
    • Pace, C. S., et al. Bispecific antibodies directed to CD4 domain 2 and HIV envelope exhibit exceptional breadth and picomolar potency against HIV-1. Proc. Natl Acad. Sci. U.S.A. 110, 13540-13545 (2013).
    • (2013) Proc. Natl Acad. Sci. U.S.A. , vol.110 , pp. 13540-13545
    • Pace, C.S.1
  • 102
    • 84904463520 scopus 로고    scopus 로고
    • Rational design and characterization of the novel, broad and potent bispecific HIV-1 neutralizing antibody iMabm36
    • Sun, M., et al. Rational design and characterization of the novel, broad and potent bispecific HIV-1 neutralizing antibody iMabm36. J. Acquir. Immune Defic. Syndr. 66, 473-483 (2014).
    • (2014) J. Acquir. Immune Defic. Syndr. , vol.66 , pp. 473-483
    • Sun, M.1
  • 103
    • 76349122922 scopus 로고    scopus 로고
    • Structural basis of respiratory syncytial virus neutralization by motavizumab
    • McLellan, J. S., et al. Structural basis of respiratory syncytial virus neutralization by motavizumab. Nat. Struct. Mol. Biol. 17, 248-250 (2010).
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 248-250
    • McLellan, J.S.1
  • 104
    • 84930474353 scopus 로고    scopus 로고
    • New options in the treatment of respiratory syncytial virus disease
    • Mejias, A., Ramilo, O. New options in the treatment of respiratory syncytial virus disease. J. Infect. 71, S80-87 (2015).
    • (2015) J. Infect. , vol.71 , pp. S80-87
    • Mejias, A.1    Ramilo, O.2
  • 105
    • 20444363121 scopus 로고    scopus 로고
    • Ultra-potent antibodies against respiratory syncytial virus: Effects of binding kinetics and binding valence on viral neutralization
    • Wu, H., et al. Ultra-potent antibodies against respiratory syncytial virus: Effects of binding kinetics and binding valence on viral neutralization. J. Mol. Biol. 350, 126-144 (2005).
    • (2005) J. Mol. Biol. , vol.350 , pp. 126-144
    • Wu, H.1
  • 106
    • 74049097923 scopus 로고    scopus 로고
    • Motavizumab for prophylaxis of respiratory syncytial virus in high-risk children: A noninferiority trial
    • Carbonell-Estrany, X., et al. Motavizumab for prophylaxis of respiratory syncytial virus in high-risk children: A noninferiority trial. Pediatrics 125, e35-51 (2010).
    • (2010) Pediatrics , vol.125 , pp. e35-51
    • Carbonell-Estrany, X.1
  • 107
    • 84887418713 scopus 로고    scopus 로고
    • A novel investigational Fc-modified humanized monoclonal antibody, motavizumab-YTE, has an extended half-life in healthy adults
    • Robbie, G. J., et al. A novel investigational Fc-modified humanized monoclonal antibody, motavizumab-YTE, has an extended half-life in healthy adults. Antimicrob. Agents Chemother. 57, 6147-6153 (2013).
    • (2013) Antimicrob. Agents Chemother. , vol.57 , pp. 6147-6153
    • Robbie, G.J.1
  • 108
    • 85014082995 scopus 로고    scopus 로고
    • Safety, tolerability, and pharmacokinetics of the respiratory syncytial virus-prefusion F-targeting monoclonal antibody with an extended half-life, MEDI8897, in healthy adults
    • Griffin, M. P., et al. Safety, tolerability, and pharmacokinetics of the respiratory syncytial virus-prefusion F-targeting monoclonal antibody with an extended half-life, MEDI8897, in healthy adults. Antimicrob Agents Chemother, doi: 10.1128/AAC.01714-16 (2016).
    • (2016) Antimicrob Agents Chemother
    • Griffin, M.P.1
  • 111
    • 84930806483 scopus 로고    scopus 로고
    • Respiratory syncytial virus, an ongoing medical dilemma: An expert commentary on respiratory syncytial virus prophylactic and therapeutic pharmaceuticals currently in clinical trials
    • Broadbent, L., Groves, H., Shields, M. D., Power, U. F. Respiratory syncytial virus, an ongoing medical dilemma: An expert commentary on respiratory syncytial virus prophylactic and therapeutic pharmaceuticals currently in clinical trials. Influenza Other Respir. Viruses 9, 169-178 (2015).
    • (2015) Influenza Other Respir. Viruses , vol.9 , pp. 169-178
    • Broadbent, L.1    Groves, H.2    Shields, M.D.3    Power, U.F.4
  • 112
    • 84992109033 scopus 로고    scopus 로고
    • Understanding Ebola: The 2014 epidemic
    • Kaner, J., Schaack, S. Understanding Ebola: The 2014 epidemic. Global. Health 12, 53 (2016).
    • (2016) Global. Health , vol.12 , pp. 53
    • Kaner, J.1    Schaack, S.2
  • 113
    • 84907263545 scopus 로고    scopus 로고
    • Reversion of advanced Ebola virus disease in nonhuman primates with ZMapp
    • Qiu, X., et al. Reversion of advanced Ebola virus disease in nonhuman primates with ZMapp. Nature 514, 47-53 (2014).
    • (2014) Nature , vol.514 , pp. 47-53
    • Qiu, X.1
  • 114
    • 84974653208 scopus 로고    scopus 로고
    • Design of a randomized controlled trial for Ebola virus disease medical countermeasures: PREVAIL II, the Ebola MCM Study
    • Dodd, L. E., et al. Design of a randomized controlled trial for Ebola virus disease medical countermeasures: PREVAIL II, the Ebola MCM Study. J. Infect. Dis. 213, 1906-1913 (2016).
    • (2016) J. Infect. Dis. , vol.213 , pp. 1906-1913
    • Dodd, L.E.1
  • 115
    • 84991259720 scopus 로고    scopus 로고
    • A randomized, controlled trial of ZMapp for Ebola virus infection
    • Group, P. I. W., Multi-National, P. I. I. S. T. A randomized, controlled trial of ZMapp for Ebola virus infection. N. Engl. J. Med. 375, 1448-1456 (2016).
    • (2016) N. Engl. J. Med. , vol.375 , pp. 1448-1456
    • Multi-National, P.I.I.S.T.1
  • 117
    • 84975256732 scopus 로고    scopus 로고
    • Potent neutralizing monoclonal antibodies against Ebola virus infection
    • Zhang, Q., et al. Potent neutralizing monoclonal antibodies against Ebola virus infection. Sci. Rep. 6, 25856 (2016).
    • (2016) Sci. Rep. , vol.6 , pp. 25856
    • Zhang, Q.1
  • 118
    • 84960400876 scopus 로고    scopus 로고
    • Isolation of potent neutralizing antibodies from a survivor of the 2014 Ebola virus outbreak
    • Bornholdt, Z. A., et al. Isolation of potent neutralizing antibodies from a survivor of the 2014 Ebola virus outbreak. Science 351, 1078-1083 (2016).
    • (2016) Science , vol.351 , pp. 1078-1083
    • Bornholdt, Z.A.1
  • 119
    • 85010933967 scopus 로고    scopus 로고
    • Zika virus infection as a cause of congenital brain abnormalities and Guillain-Barre syndrome: Systematic review
    • Krauer, F., et al. zika virus infection as a cause of congenital brain abnormalities and Guillain-Barre syndrome: Systematic review. PLoS Med. 14, e1002203 (2017).
    • (2017) PLoS Med. , vol.14 , pp. e1002203
    • Krauer, F.1
  • 120
    • 85015806084 scopus 로고    scopus 로고
    • Research and development of Zika virus vaccines
    • Dawes, B. E., et al. Research and development of Zika virus vaccines. Npj Vaccines 1, 16007, doi: 10.1038/npjvaccines.2016.7 (2016).
    • (2016) Npj Vaccines , vol.1 , pp. 16007
    • Dawes, B.E.1
  • 121
    • 84929483927 scopus 로고    scopus 로고
    • Estimating the global burden of endemic canine rabies
    • Hampson, K., et al. Estimating the global burden of endemic canine rabies. PLoS Negl. Trop. Dis. 9, e0003709 (2015).
    • (2015) PLoS Negl. Trop. Dis. , vol.9 , pp. e0003709
    • Hampson, K.1
  • 122
  • 123
    • 55049129776 scopus 로고    scopus 로고
    • First administration to humans of a monoclonal antibody cocktail against rabies virus: Safety, tolerability, and neutralizing activity
    • Bakker, A. B., et al. First administration to humans of a monoclonal antibody cocktail against rabies virus: Safety, tolerability, and neutralizing activity. Vaccine 26, 5922-5927 (2008).
    • (2008) Vaccine , vol.26 , pp. 5922-5927
    • Bakker, A.B.1
  • 124
    • 0025369456 scopus 로고
    • Biological characterization of human monoclonal antibodies to rabies virus
    • Dietzschold, B., et al. Biological characterization of human monoclonal antibodies to rabies virus. J. Virol. 64, 3087-3090 (1990).
    • (1990) J. Virol. , vol.64 , pp. 3087-3090
    • Dietzschold, B.1
  • 125
    • 20144388644 scopus 로고    scopus 로고
    • Novel rabies virus-neutralizing epitope recognized by human monoclonal antibody: Fine mapping and escape mutant analysis
    • Marissen, W. E., et al. Novel rabies virus-neutralizing epitope recognized by human monoclonal antibody: Fine mapping and escape mutant analysis. J. Virol. 79, 4672-4678 (2005).
    • (2005) J. Virol. , vol.79 , pp. 4672-4678
    • Marissen, W.E.1
  • 126
    • 21644487726 scopus 로고    scopus 로고
    • Novel human monoclonal antibody combination effectively neutralizing natural rabies virus variants and individual in vitro escape mutants
    • Bakker, A. B., et al. Novel human monoclonal antibody combination effectively neutralizing natural rabies virus variants and individual in vitro escape mutants. J. Virol. 79, 9062-9068 (2005).
    • (2005) J. Virol. , vol.79 , pp. 9062-9068
    • Bakker, A.B.1
  • 130
    • 33947134318 scopus 로고    scopus 로고
    • Identification and characterization of a human monoclonal antibody that potently neutralizes a broad panel of rabies virus isolates
    • Sloan, S. E., et al. Identification and characterization of a human monoclonal antibody that potently neutralizes a broad panel of rabies virus isolates. Vaccine 25, 2800-2810 (2007).
    • (2007) Vaccine , vol.25 , pp. 2800-2810
    • Sloan, S.E.1
  • 131
    • 79959698307 scopus 로고    scopus 로고
    • G glycoprotein amino acid residues required for human monoclonal antibody RAB1 neutralization are conserved in rabies virus street isolates
    • Wang, Y., et al. G glycoprotein amino acid residues required for human monoclonal antibody RAB1 neutralization are conserved in rabies virus street isolates. Antiviral Res. 91, 187-194 (2011).
    • (2011) Antiviral Res. , vol.91 , pp. 187-194
    • Wang, Y.1
  • 132
    • 84961282543 scopus 로고    scopus 로고
    • Development of broad-spectrum human monoclonal antibodies for rabies post-exposure prophylaxis
    • De Benedictis, P., et al. Development of broad-spectrum human monoclonal antibodies for rabies post-exposure prophylaxis. EMBO Mol. Med. 8, 407-421 (2016).
    • (2016) EMBO Mol. Med. , vol.8 , pp. 407-421
    • De Benedictis, P.1
  • 134
    • 84962045286 scopus 로고    scopus 로고
    • Prolonged suppression of HBV in mice by a novel antibody that targets a unique epitope on hepatitis B surface antigen
    • Zhang, T. Y., et al. Prolonged suppression of HBV in mice by a novel antibody that targets a unique epitope on hepatitis B surface antigen. Gut 65, 658-671 (2016).
    • (2016) Gut , vol.65 , pp. 658-671
    • Zhang, T.Y.1
  • 135
    • 84961205301 scopus 로고    scopus 로고
    • A human monoclonal antibody against small envelope protein of hepatitis B virus with potent neutralization effect
    • Wang, W., et al. A human monoclonal antibody against small envelope protein of hepatitis B virus with potent neutralization effect. MAbs 8, 468-477 (2016).
    • (2016) MAbs , vol.8 , pp. 468-477
    • Wang, W.1
  • 136
    • 84957603435 scopus 로고    scopus 로고
    • The development of therapeutic antibodies against dengue virus
    • Fibriansah, G., Lok, S. M. The development of therapeutic antibodies against dengue virus. Antiviral Res. 128, 7-19 (2016).
    • (2016) Antiviral Res. , vol.128 , pp. 7-19
    • Fibriansah, G.1    Lok, S.M.2
  • 137
    • 80052496440 scopus 로고    scopus 로고
    • Critical issues in dengue vaccine development
    • Thomas, S. J., Endy, T. P. Critical issues in dengue vaccine development. Curr. Opin. Infect. Dis. 24, 442-450 (2011).
    • (2011) Curr. Opin. Infect. Dis. , vol.24 , pp. 442-450
    • Thomas, S.J.1    Endy, T.P.2
  • 138
    • 79961023581 scopus 로고    scopus 로고
    • Cytomegalovirus-induced immunopathology and its clinical consequences
    • Varani, S., Landini, M. P. Cytomegalovirus-induced immunopathology and its clinical consequences. Herpesviridae 2, 6 (2011).
    • (2011) Herpesviridae , vol.2 , pp. 6
    • Varani, S.1    Landini, M.P.2
  • 139
    • 15244343878 scopus 로고    scopus 로고
    • Dengue virus infections: Comparison of methods for diagnosing the acute disease
    • de Oliveira Poersch, C., et al. Dengue virus infections: Comparison of methods for diagnosing the acute disease. J. Clin. Virol. 32, 272-277 (2005).
    • (2005) J. Clin. Virol. , vol.32 , pp. 272-277
    • De Oliveira Poersch, C.1
  • 140
    • 84988726145 scopus 로고    scopus 로고
    • Dengue in the context of the integrated management of childhood illness
    • Deen, J., Weber, M. W., Jaenisch, T. Dengue in the context of the integrated management of childhood illness. PLoS Negl. Trop. Dis. 10, e0004838 (2016).
    • (2016) PLoS Negl. Trop. Dis. , vol.10 , pp. e0004838
    • Deen, J.1    Weber, M.W.2    Jaenisch, T.3
  • 141
    • 84948706705 scopus 로고    scopus 로고
    • New insights into the immunopathology and control of dengue virus infection
    • Screaton, G., Mongkolsapaya, J., Yacoub, S., Roberts, C. New insights into the immunopathology and control of dengue virus infection. Nat. Rev. Immunol. 15, 745-759 (2015).
    • (2015) Nat. Rev. Immunol. , vol.15 , pp. 745-759
    • Screaton, G.1    Mongkolsapaya, J.2    Yacoub, S.3    Roberts, C.4
  • 142
    • 84935097021 scopus 로고    scopus 로고
    • Cryo-EM structure of an antibody that neutralizes dengue virus type 2 by locking E protein dimers
    • DENGUE VIRUS.
    • Fibriansah, G., et al. DENGUE VIRUS. Cryo-EM structure of an antibody that neutralizes dengue virus type 2 by locking E protein dimers. Science 349, 88-91 (2015).
    • (2015) Science , vol.349 , pp. 88-91
    • Fibriansah, G.1
  • 143
    • 84895752114 scopus 로고    scopus 로고
    • A potent anti-dengue human antibody preferentially recognizes the conformation of E protein monomers assembled on the virus surface
    • Fibriansah, G., et al. A potent anti-dengue human antibody preferentially recognizes the conformation of E protein monomers assembled on the virus surface. EMBO Mol. Med. 6, 358-371 (2014).
    • (2014) EMBO Mol. Med. , vol.6 , pp. 358-371
    • Fibriansah, G.1
  • 144
    • 36349025356 scopus 로고    scopus 로고
    • Epitope determinants of a chimpanzee dengue virus type 4 (DENV-4)-neutralizing antibody and protection against DENV-4 challenge in mice and rhesus monkeys by passively transferred humanized antibody
    • Lai, C. J., et al. Epitope determinants of a chimpanzee dengue virus type 4 (DENV-4)-neutralizing antibody and protection against DENV-4 challenge in mice and rhesus monkeys by passively transferred humanized antibody. J. Virol. 81, 12766-12774 (2007).
    • (2007) J. Virol. , vol.81 , pp. 12766-12774
    • Lai, C.J.1
  • 145
    • 77954039828 scopus 로고    scopus 로고
    • The development of therapeutic antibodies that neutralize homologous and heterologous genotypes of dengue virus type 1
    • 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).
    • (2010) PLoS Pathog. , vol.6 , pp. e1000823
    • Shrestha, B.1
  • 146
    • 84862850400 scopus 로고    scopus 로고
    • The structural basis for serotype-specific neutralization of dengue virus by a human antibody
    • Teoh, E. P., et al. The structural basis for serotype-specific neutralization of dengue virus by a human antibody. Sci. Transl. Med. 4, 139ra183 (2012).
    • (2012) Sci. Transl. Med. , vol.4 , pp. 139-183
    • Teoh, E.P.1
  • 147
    • 84891619354 scopus 로고    scopus 로고
    • The potent and broadly neutralizing human dengue virus-specific monoclonal antibody 1C19 reveals a unique cross-reactive epitope on the bc loop of domain II of the envelope protein
    • Smith, S. A., et al. The potent and broadly neutralizing human dengue virus-specific monoclonal antibody 1C19 reveals a unique cross-reactive epitope on the bc loop of domain II of the envelope protein. mBio 4, e00873-00813 (2013).
    • (2013) MBio , vol.4 , pp. e00873-e00813
    • Smith, S.A.1
  • 148
    • 84938422733 scopus 로고    scopus 로고
    • Structure-guided design of an anti-dengue antibody directed to a non-immunodominant epitope
    • Robinson, L. N., et al. Structure-guided design of an anti-dengue antibody directed to a non-immunodominant epitope. Cell 162, 493-504 (2015).
    • (2015) Cell , vol.162 , pp. 493-504
    • Robinson, L.N.1
  • 149
    • 84874766259 scopus 로고    scopus 로고
    • Therapeutic efficacy of antibodies lacking Fcgamma receptor binding against lethal dengue virus infection is due to neutralizing potency and blocking of enhancing antibodies [corrected]
    • Williams, K. L., et al. Therapeutic efficacy of antibodies lacking Fcgamma receptor binding against lethal dengue virus infection is due to neutralizing potency and blocking of enhancing antibodies [corrected]. PLoS Pathog. 9, e1003157 (2013).
    • (2013) PLoS Pathog. , vol.9 , pp. e1003157
    • Williams, K.L.1
  • 150
    • 84946907363 scopus 로고    scopus 로고
    • Antibody with an engineered Fc region as a therapeutic agent against dengue virus infection
    • Ramadhany, R., et al. Antibody with an engineered Fc region as a therapeutic agent against dengue virus infection. Antiviral Res. 124, 61-68 (2015).
    • (2015) Antiviral Res. , vol.124 , pp. 61-68
    • Ramadhany, R.1
  • 151
    • 77956605864 scopus 로고    scopus 로고
    • The human immune response to Dengue virus is dominated by highly cross-reactive antibodies endowed with neutralizing and enhancing activity
    • Beltramello, M., et al. The human immune response to Dengue virus is dominated by highly cross-reactive antibodies endowed with neutralizing and enhancing activity. Cell Host Microbe 8, 271-283 (2010).
    • (2010) Cell Host Microbe , vol.8 , pp. 271-283
    • Beltramello, M.1
  • 152
    • 84875237748 scopus 로고    scopus 로고
    • Monoclonal antibodies for prophylactic and therapeutic use against viral infections
    • Both, L., et al. Monoclonal antibodies for prophylactic and therapeutic use against viral infections. Vaccine 31, 1553-1559 (2013).
    • (2013) Vaccine , vol.31 , pp. 1553-1559
    • Both, L.1
  • 153
    • 85037843607 scopus 로고    scopus 로고
    • Rabies control: Could innovative financing break the deadlock?
    • Welburn, S. C., Coleman, P. G., Zinsstag, J. Rabies control: Could innovative financing break the deadlock? Front. Vet. Sci. 4, 32 (2017).
    • (2017) Front. Vet. Sci. , vol.4 , pp. 32
    • Welburn, S.C.1    Coleman, P.G.2    Zinsstag, J.3
  • 155
    • 85010900171 scopus 로고    scopus 로고
    • Anti-retroviral antibody FcgammaR-mediated effector functions
    • Bournazos, S., Ravetch, J. V. Anti-retroviral antibody FcgammaR-mediated effector functions. Immunol. Rev. 275, 285-295 (2017).
    • (2017) Immunol. Rev. , vol.275 , pp. 285-295
    • Bournazos, S.1    Ravetch, J.V.2
  • 156
    • 84936935341 scopus 로고    scopus 로고
    • Engineering humoral immunity as prophylaxis or therapy
    • Deal, C. E., Balazs, A. B. Engineering humoral immunity as prophylaxis or therapy. Curr. Opin. Immunol. 35, 113-122 (2015).
    • (2015) Curr. Opin. Immunol. , vol.35 , pp. 113-122
    • Deal, C.E.1    Balazs, A.B.2
  • 157
    • 84938244572 scopus 로고    scopus 로고
    • Protection against dengue disease by synthetic nucleic acid antibody prophylaxis/immunotherapy
    • Flingai, S., et al. Protection against dengue disease by synthetic nucleic acid antibody prophylaxis/immunotherapy. Sci. Rep. 5, 12616 (2015).
    • (2015) Sci. Rep. , vol.5 , pp. 12616
    • Flingai, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.