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Volumn 11, Issue 5, 2005, Pages 522-530

Development of a humanized monoclonal antibody with therapeutic potential against West Nile virus

Author keywords

[No Author keywords available]

Indexed keywords

MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY E16; MONOCLONAL ANTIBODY E24; MONOCLONAL ANTIBODY E27; MONOCLONAL ANTIBODY E33; MONOCLONAL ANTIBODY E34; MONOCLONAL ANTIBODY E40; MONOCLONAL ANTIBODY E43; MONOCLONAL ANTIBODY E47; MONOCLONAL ANTIBODY E49; MONOCLONAL ANTIBODY E58; NEUTRALIZING ANTIBODY; UNCLASSIFIED DRUG; VIRUS ANTIBODY; VIRUS ENVELOPE PROTEIN;

EID: 21044448356     PISSN: 10788956     EISSN: None     Source Type: Journal    
DOI: 10.1038/nm1240     Document Type: Article
Times cited : (452)

References (47)
  • 1
    • 4344647820 scopus 로고    scopus 로고
    • West Nile virus: Where are we now?
    • Granwehr, B.P. et al. West Nile virus: where are we now? Lancet Infect. Dis. 4, 547-556 (2004).
    • (2004) Lancet Infect. Dis. , vol.4 , pp. 547-556
    • Granwehr, B.P.1
  • 2
    • 0141925650 scopus 로고    scopus 로고
    • Innate and adaptive immune responses determine protection against disseminated infection by West Nile Encephalitis virus
    • Diamond, M.S., Shrestha, B., Mehlhop, E., Sitati, E. & Engle, M. Innate and adaptive immune responses determine protection against disseminated infection by West Nile Encephalitis virus. Viral Immunol. 16, 259-278 (2003).
    • (2003) Viral Immunol. , vol.16 , pp. 259-278
    • Diamond, M.S.1    Shrestha, B.2    Mehlhop, E.3    Sitati, E.4    Engle, M.5
  • 3
    • 3042854213 scopus 로고    scopus 로고
    • Immunity to West Nile virus
    • Wang, T. & Fikrig, E. Immunity to West Nile virus. Curr. Opin. Immunol. 16, 519-523 (2004).
    • (2004) Curr. Opin. Immunol. , vol.16 , pp. 519-523
    • Wang, T.1    Fikrig, E.2
  • 4
    • 0038448987 scopus 로고    scopus 로고
    • Prophylactic and therapeutic efficacy of human intravenous immunoglobulin in treating west nile virus infection in mice
    • Ben-Nathan, D. et al. Prophylactic and therapeutic efficacy of human intravenous immunoglobulin in treating west nile virus infection in mice. J. Infect. Dis. 188, 5-12 (2003).
    • (2003) J. Infect. Dis. , vol.188 , pp. 5-12
    • Ben-Nathan, D.1
  • 5
    • 0344304693 scopus 로고    scopus 로고
    • Antibody prophylaxis and therapy against West Nile Virus infection in wild type and immunodeficient mice
    • Engle, M. & Diamond, M.S. Antibody prophylaxis and therapy against West Nile Virus infection in wild type and immunodeficient mice. J. Virol. 77, 12941-12949 (2003).
    • (2003) J. Virol. , vol.77 , pp. 12941-12949
    • Engle, M.1    Diamond, M.S.2
  • 7
    • 0037495036 scopus 로고    scopus 로고
    • A ligand-binding pocket in the dengue virus envelope glycoprotein
    • Modis, Y., Ogata, S., Clements, D. & Harrison, S.C. A ligand-binding pocket in the dengue virus envelope glycoprotein. Proc. Natl. Acad. Sci. USA 100, 6986-6991 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6986-6991
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 8
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 Angstrom resolution
    • Rey, F.A., Heinz, F.X., Mandl, C., Kunz, C. & Harrison, S.C. The envelope glycoprotein from tick-borne encephalitis virus at 2 Angstrom resolution. Nature 315, 291-298 (1995).
    • (1995) Nature , vol.315 , pp. 291-298
    • Rey, F.A.1    Heinz, F.X.2    Mandl, C.3    Kunz, C.4    Harrison, S.C.5
  • 9
    • 0038810275 scopus 로고    scopus 로고
    • Dengue virus envelope glycoprotein structure: New insight into its interactions during viral entry
    • Rey, F.A. Dengue virus envelope glycoprotein structure: new insight into its interactions during viral entry. Proc. Natl. Acad. Sci. USA 100, 6899-6901 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6899-6901
    • Rey, F.A.1
  • 10
    • 1642499388 scopus 로고    scopus 로고
    • Structure of the dengue virus envelope protein after membrane fusion
    • Modis, Y., Ogata, S., Clements, D. & Harrison, S.C. Structure of the dengue virus envelope protein after membrane fusion. Nature 427, 313-319 (2004).
    • (2004) Nature , vol.427 , pp. 313-319
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 11
    • 0242574743 scopus 로고    scopus 로고
    • Visualization of membrane protein domains by cryo-electron microscopy of dengue virus
    • Zhang, W. et al. Visualization of membrane protein domains by cryo-electron microscopy of dengue virus. Nat. Struct. Biol. 10, 907-912 (2003).
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 907-912
    • Zhang, W.1
  • 13
    • 0035088293 scopus 로고    scopus 로고
    • Biophysical characterization and vector-specific antagonist activity of domain III of the tick-borne flavivirus envelope protein
    • Bhardwaj, S., Holbrook, M., Shope, R.E., Barrett, A.D. & Watowich, S.J. Biophysical characterization and vector-specific antagonist activity of domain III of the tick-borne flavivirus envelope protein. J. Virol. 75, 4002-4007 (2001).
    • (2001) J. Virol. , vol.75 , pp. 4002-4007
    • Bhardwaj, S.1    Holbrook, M.2    Shope, R.E.3    Barrett, A.D.4    Watowich, S.J.5
  • 14
    • 13644262812 scopus 로고    scopus 로고
    • Inhibition of West Nile virus entry by using a recombinant domain III from the envelope glycoprotein
    • Chu, J.J. et al. Inhibition of West Nile virus entry by using a recombinant domain III from the envelope glycoprotein. J. Gen. Virol. 86, 405-412 (2005).
    • (2005) J. Gen. Virol. , vol.86 , pp. 405-412
    • Chu, J.J.1
  • 15
    • 0036891872 scopus 로고    scopus 로고
    • Identification of neutralizing epitopes within structural domain III of the West Nile virus envelope protein
    • Beasley, D.W. & Barrett, A.D. Identification of neutralizing epitopes within structural domain III of the West Nile virus envelope protein. J. Virol. 76, 13097-13100 (2002).
    • (2002) J. Virol. , vol.76 , pp. 13097-13100
    • Beasley, D.W.1    Barrett, A.D.2
  • 16
    • 4644372800 scopus 로고    scopus 로고
    • Solution structure and antibody binding studies of the envelope protein domain III from the New York strain of West Nile virus
    • Volk, D.E. et al. Solution structure and antibody binding studies of the envelope protein domain III from the New York strain of West Nile virus. J. Biol. Chem. 279, 38755-38761 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 38755-38761
    • Volk, D.E.1
  • 17
    • 0035864283 scopus 로고    scopus 로고
    • Epitopes on the dengue 1 virus envelope protein recognized by neutralizing IgM monoclonal antibodies
    • Beasley, D.W. & Aaskov, J.G. Epitopes on the dengue 1 virus envelope protein recognized by neutralizing IgM monoclonal antibodies. Virology 279, 447-458 (2001).
    • (2001) Virology , vol.279 , pp. 447-458
    • Beasley, D.W.1    Aaskov, J.G.2
  • 18
    • 0034899311 scopus 로고    scopus 로고
    • Monoclonal antibodies that bind to domain III of dengue virus E glycoprotein are the most efficient blockers of virus adsorption to Vero cells
    • Crill, W.D. & Roehrig, J.T. Monoclonal antibodies that bind to domain III of dengue virus E glycoprotein are the most efficient blockers of virus adsorption to Vero cells. J. Virol. 75, 7769-7773 (2001).
    • (2001) J. Virol. , vol.75 , pp. 7769-7773
    • Crill, W.D.1    Roehrig, J.T.2
  • 19
    • 0032486594 scopus 로고    scopus 로고
    • Monoclonal antibody mapping of the envelope glycoprotein of the dengue 2 virus, Jamaica
    • Roehrig, J.T., Bolin, R.A. & Kelly, R.G. Monoclonal antibody mapping of the envelope glycoprotein of the dengue 2 virus, Jamaica. Virology 246, 317-328 (1998).
    • (1998) Virology , vol.246 , pp. 317-328
    • Roehrig, J.T.1    Bolin, R.A.2    Kelly, R.G.3
  • 20
    • 0025981170 scopus 로고
    • Nucleotide changes responsible for loss of neuroinvasiveness in Japanese encephalitis virus neutralization-resistant mutants
    • Cecilia, D. & Gould, E.A. Nucleotide changes responsible for loss of neuroinvasiveness in Japanese encephalitis virus neutralization-resistant mutants. Virology 181, 70-77 (1991).
    • (1991) Virology , vol.181 , pp. 70-77
    • Cecilia, D.1    Gould, E.A.2
  • 21
    • 0031259847 scopus 로고    scopus 로고
    • Japanese encephalitis virus antigenic variants with characteristic differences in neutralization resistance and mouse virulence
    • Wu, S.C., Lian, W.C., Hsu, L.C. & Liau, M.Y. Japanese encephalitis virus antigenic variants with characteristic differences in neutralization resistance and mouse virulence. Virus Res. 51, 173-181 (1997).
    • (1997) Virus Res. , vol.51 , pp. 173-181
    • Wu, S.C.1    Lian, W.C.2    Hsu, L.C.3    Liau, M.Y.4
  • 22
    • 0028059533 scopus 로고
    • Localization of a neutralizing epitope on the envelope protein of dengue virus type 2
    • Lin, B., Parrish, C.R., Murray, J.M. & Wright, P.J. Localization of a neutralizing epitope on the envelope protein of dengue virus type 2. Virology 202, 885-890 (1994).
    • (1994) Virology , vol.202 , pp. 885-890
    • Lin, B.1    Parrish, C.R.2    Murray, J.M.3    Wright, P.J.4
  • 23
    • 0037319970 scopus 로고    scopus 로고
    • B cells and antibody play critical roles in the immediate defense of disseminated infection by West Nile encephalitis virus
    • Diamond, M.S., Shrestha, B., Marri, A., Mahan, D. & Engle, M. B cells and antibody play critical roles in the immediate defense of disseminated infection by West Nile encephalitis virus. J. Virol. 77, 2578-2586 (2003).
    • (2003) J. Virol. , vol.77 , pp. 2578-2586
    • Diamond, M.S.1    Shrestha, B.2    Marri, A.3    Mahan, D.4    Engle, M.5
  • 25
    • 0030994634 scopus 로고    scopus 로고
    • Yeast surface display for screening combinatorial polypeptide libraries
    • Boder, E.T. & Wittrup, K.D. Yeast surface display for screening combinatorial polypeptide libraries. Nat. Biotechnol. 15, 553-557 (1997).
    • (1997) Nat. Biotechnol. , vol.15 , pp. 553-557
    • Boder, E.T.1    Wittrup, K.D.2
  • 26
    • 0342530626 scopus 로고
    • Mouse/human chimeric monoclonal antibody in man: Kinetics and immune response
    • LoBuglio, A.F. et al. Mouse/human chimeric monoclonal antibody in man: kinetics and immune response. Proc. Natl. Acad. Sci. USA 86, 4220-4224 (1989).
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4220-4224
    • LoBuglio, A.F.1
  • 27
    • 0025776895 scopus 로고
    • Pharmacokinetics, immune response, and biodistribution of iodine-131-labeled chimeric mouse/human IgG1,k 17-1A monoclonal antibody
    • Meredith, R.F. et al. Pharmacokinetics, immune response, and biodistribution of iodine-131-labeled chimeric mouse/human IgG1,k 17-1A monoclonal antibody. J. Nucl. Med. 32, 1162-1168 (1991).
    • (1991) J. Nucl. Med. , vol.32 , pp. 1162-1168
    • Meredith, R.F.1
  • 28
    • 0024438061 scopus 로고
    • Studies of aglycosylated chimeric mouse-human IgG. Role of carbohydrate in the structure and effector functions mediated by the human IgG constant region
    • Tao, M.H. & Morrison, S.L. Studies of aglycosylated chimeric mouse-human IgG. Role of carbohydrate in the structure and effector functions mediated by the human IgG constant region. J. Immunol. 143, 2595-2601 (1989).
    • (1989) J. Immunol. , vol.143 , pp. 2595-2601
    • Tao, M.H.1    Morrison, S.L.2
  • 30
    • 0031714337 scopus 로고    scopus 로고
    • West Nile virus envelope proteins: Nucleotide sequence analysis of strains differing in mouse neuroinvasiveness
    • Chambers, T.J., Halevy, M., Nestorowicz, A., Rice, C.M. & Lustig, S. West Nile virus envelope proteins: nucleotide sequence analysis of strains differing in mouse neuroinvasiveness. J. Gen. Virol. 79, 2375-2380 (1998).
    • (1998) J. Gen. Virol. , vol.79 , pp. 2375-2380
    • Chambers, T.J.1    Halevy, M.2    Nestorowicz, A.3    Rice, C.M.4    Lustig, S.5
  • 31
    • 0242580241 scopus 로고    scopus 로고
    • Structural basis of a Flavivirus recognized by its neutralizing antibody: Solution structure of the domain III of the Japanese Encephalitis virus envelope protein
    • Wu, K.P. et al. Structural basis of a Flavivirus recognized by its neutralizing antibody: Solution structure of the domain III of the Japanese Encephalitis virus envelope protein. J. Biol. Chem. 278, 46007-46013 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 46007-46013
    • Wu, K.P.1
  • 32
    • 0023716351 scopus 로고
    • Protection of mice against Japanese encephalitis virus by passive administration with monoclonal antibodies
    • Kimura-Kuroda, J. & Yasui, K. Protection of mice against Japanese encephalitis virus by passive administration with monoclonal antibodies. J. Immunol. 141, 3606-3610 (1988).
    • (1988) J. Immunol. , vol.141 , pp. 3606-3610
    • Kimura-Kuroda, J.1    Yasui, K.2
  • 33
    • 0024202233 scopus 로고
    • Antibody protects against lethal infection with the neurally spreading reovirus type 3 (Dearing)
    • Virgin, H.W., Bassel-Duby, R., Fields, B.N. & Tyler, K.L. Antibody protects against lethal infection with the neurally spreading reovirus type 3 (Dearing). J. Virol. 62, 4594-4604 (1988).
    • (1988) J. Virol. , vol.62 , pp. 4594-4604
    • Virgin, H.W.1    Bassel-Duby, R.2    Fields, B.N.3    Tyler, K.L.4
  • 34
    • 0026354236 scopus 로고
    • Antibody-mediated clearance of alphavirus infection from neurons
    • Levine, B. et al. Antibody-mediated clearance of alphavirus infection from neurons. Science 254, 856-860 (1991).
    • (1991) Science , vol.254 , pp. 856-860
    • Levine, B.1
  • 35
    • 0034101043 scopus 로고    scopus 로고
    • Modulation of dengue virus infection in human cells by alpha, beta, and gamma interferons
    • Diamond, M. et al. Modulation of dengue virus infection in human cells by alpha, beta, and gamma interferons. J. Virol. 74, 4957-4966 (2000).
    • (2000) J. Virol. , vol.74 , pp. 4957-4966
    • Diamond, M.1
  • 38
    • 0028302115 scopus 로고
    • Analysis of C-terminally truncated dengue 2 and dengue 3 virus envelope glycoproteins: Processing in insect cells and immunogenic properties in mice
    • Delenda, C., Staropoli, I., Frenkiel, M.P., Cabanie, L. & Deubel, V. Analysis of C-terminally truncated dengue 2 and dengue 3 virus envelope glycoproteins: processing in insect cells and immunogenic properties in mice. J. Gen. Virol. 75, 1569-1578 (1994).
    • (1994) J. Gen. Virol. , vol.75 , pp. 1569-1578
    • Delenda, C.1    Staropoli, I.2    Frenkiel, M.P.3    Cabanie, L.4    Deubel, V.5
  • 39
    • 0033579282 scopus 로고    scopus 로고
    • Origin of the West Nile virus responsible for an outbreak of encephalitis in the northeastern United States
    • Lanciotti, R.S. et al. Origin of the West Nile virus responsible for an outbreak of encephalitis in the northeastern United States. Science 286, 2333-2337 (1999).
    • (1999) Science , vol.286 , pp. 2333-2337
    • Lanciotti, R.S.1
  • 40
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Harlow, E. & Lane, D. Antibodies: A Laboratory Manual, p. 714 (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, 1988).
    • (1988) Antibodies: A Laboratory Manual , pp. 714
    • Harlow, E.1    Lane, D.2
  • 41
    • 2642711705 scopus 로고    scopus 로고
    • Optimal screening of surface-displayed polypeptide libraries
    • Boder, E.T. & Wittrup, K.D. Optimal screening of surface-displayed polypeptide libraries. Biotechnol. Prog. 14, 55-62 (1998).
    • (1998) Biotechnol. Prog. , vol.14 , pp. 55-62
    • Boder, E.T.1    Wittrup, K.D.2
  • 43
    • 0031775443 scopus 로고    scopus 로고
    • The complete nucleotide sequence of the human immunoglobulin heavy chain variable region locus
    • Matsuda, F. et al. The complete nucleotide sequence of the human immunoglobulin heavy chain variable region locus. J. Exp. Med. 188, 2151-2162 (1998).
    • (1998) J. Exp. Med. , vol.188 , pp. 2151-2162
    • Matsuda, F.1
  • 44
    • 0019846077 scopus 로고
    • Structure of the human immunoglobulin mu locus: Characterization of embryonic and rearranged J and D genes
    • Ravetch, J.V., Siebenlist, U., Korsmeyer, S., Waldmann, T. & Leder, P. Structure of the human immunoglobulin mu locus: characterization of embryonic and rearranged J and D genes. Cell 27, 583-591 (1981).
    • (1981) Cell , vol.27 , pp. 583-591
    • Ravetch, J.V.1    Siebenlist, U.2    Korsmeyer, S.3    Waldmann, T.4    Leder, P.5
  • 46
    • 0022432374 scopus 로고
    • Subgroup IV of human immunoglobulin K light chains is encoded by a single germline gene
    • Klobeck, H.G. et al. Subgroup IV of human immunoglobulin K light chains is encoded by a single germline gene. Nucleic Acids Res. 13, 6515-6529 (1985).
    • (1985) Nucleic Acids Res. , vol.13 , pp. 6515-6529
    • Klobeck, H.G.1
  • 47
    • 0020051098 scopus 로고
    • Evolution of human immunoglobulin kappa J region genes
    • Hieter, P.A., Maizel, J.V., Jr. & Leder, P. Evolution of human immunoglobulin kappa J region genes. J. Biol. Chem. 257, 1516-1522 (1982).
    • (1982) J. Biol. Chem. , vol.257 , pp. 1516-1522
    • Hieter, P.A.1    Maizel Jr., J.V.2    Leder, P.3


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