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On a mouse monoclonal antibody that neutralizes all four dengue virus serotypes

Identifieur interne : 002E89 ( PascalFrancis/Corpus ); précédent : 002E88; suivant : 002E90

On a mouse monoclonal antibody that neutralizes all four dengue virus serotypes

Auteurs : Ravikumar Rajamanonmani ; Celine Nkenfou ; Paula Clancy ; YIN HOE YAU ; Susana Geifman Shochat ; Soila Sukupolvi-Petty ; Wouter Schul ; Michael S. Diamond ; Subhash G. Vasudevan ; Julien Lescar

Source :

RBID : Pascal:09-0162365

Descripteurs français

English descriptors

Abstract

The flavivirus envelope glycoprotein (E) is responsible for viral attachment and entry by membrane fusion. Its ectodomain is the primary target of the humoral immune response. In particular, the C-terminal Ig-like domain III of E, which is exposed at the surface of the viral particle, forms an attractive antigen for raising protective monoclonal antibodies (mAb). 9F12, a mouse mAb raised against a dengue virus (DENV) serotype 2 recombinant domain III, cross-reacts with corresponding domains from the other three DENV serotypes and also with West Nile virus. mAb 9F1 2 binds with nanomolar affinity to a conserved epitope that maps to the viral surface comprising residues 305, 307, 310 and 330 of the E protein. mAb 9F1 2 neutralizes all four DENV serotypes in plaque reduction assays. We expressed a single-chain Fv from 9F12 that retains the binding activity of the parent mAb. Adsorption and fusion inhibition assays indicate that mAb 9F1 2 prevents early steps of viral entry. Its virus inhibition activity and broad cross-reactivity makes mAb 9F12 a suitable candidate for optimization and humanization into a therapeutic antibody to treat severe infections by dengue.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

pA  
A01 01  1    @0 0022-1317
A02 01      @0 JGVIAY
A03   1    @0 J. gen. virol.
A05       @2 90
A06       @3 p. 4
A08 01  1  ENG  @1 On a mouse monoclonal antibody that neutralizes all four dengue virus serotypes
A11 01  1    @1 RAJAMANONMANI (Ravikumar)
A11 02  1    @1 NKENFOU (Celine)
A11 03  1    @1 CLANCY (Paula)
A11 04  1    @1 YIN HOE YAU
A11 05  1    @1 GEIFMAN SHOCHAT (Susana)
A11 06  1    @1 SUKUPOLVI-PETTY (Soila)
A11 07  1    @1 SCHUL (Wouter)
A11 08  1    @1 DIAMOND (Michael S.)
A11 09  1    @1 VASUDEVAN (Subhash G.)
A11 10  1    @1 LESCAR (Julien)
A14 01      @1 School of Biological Sciences, Nanyang Technological University @2 Biopolis @3 SGP @Z 1 aut. @Z 4 aut. @Z 5 aut. @Z 10 aut.
A14 02      @1 Program in Emerging Infectious Diseases, Duke-NUS, Graduate Medical School @3 SGP @Z 1 aut. @Z 9 aut.
A14 03      @1 Novartis Institute for Tropical Diseases @2 Biopolis @3 SGP @Z 2 aut. @Z 7 aut.
A14 04      @1 Department of Biochemistry and Molecular Biology, James Cook University @3 AUS @Z 3 aut. @Z 9 aut.
A14 05      @1 Departments of Medicine, Molecular Microbiology, Pathology and Immunology, Washington University School of Medicine @2 St Louis @3 USA @Z 6 aut. @Z 8 aut.
A14 06      @1 AFMB CNRS UMR6098 @2 Marseille @3 FRA @Z 10 aut.
A20       @1 799-809
A21       @1 2009
A23 01      @0 ENG
A43 01      @1 INIST @2 13533 @5 354000187410180030
A44       @0 0000 @1 © 2009 INIST-CNRS. All rights reserved.
A45       @0 1 p.3/4
A47 01  1    @0 09-0162365
A60       @1 P
A61       @0 A
A64 01  1    @0 Journal of general virology
A66 01      @0 GBR
C01 01    ENG  @0 The flavivirus envelope glycoprotein (E) is responsible for viral attachment and entry by membrane fusion. Its ectodomain is the primary target of the humoral immune response. In particular, the C-terminal Ig-like domain III of E, which is exposed at the surface of the viral particle, forms an attractive antigen for raising protective monoclonal antibodies (mAb). 9F12, a mouse mAb raised against a dengue virus (DENV) serotype 2 recombinant domain III, cross-reacts with corresponding domains from the other three DENV serotypes and also with West Nile virus. mAb 9F1 2 binds with nanomolar affinity to a conserved epitope that maps to the viral surface comprising residues 305, 307, 310 and 330 of the E protein. mAb 9F1 2 neutralizes all four DENV serotypes in plaque reduction assays. We expressed a single-chain Fv from 9F12 that retains the binding activity of the parent mAb. Adsorption and fusion inhibition assays indicate that mAb 9F1 2 prevents early steps of viral entry. Its virus inhibition activity and broad cross-reactivity makes mAb 9F12 a suitable candidate for optimization and humanization into a therapeutic antibody to treat severe infections by dengue.
C02 01  X    @0 002A05C10
C02 02  X    @0 002A05C07
C03 01  X  FRE  @0 Souris @5 01
C03 01  X  ENG  @0 Mouse @5 01
C03 01  X  SPA  @0 Ratón @5 01
C03 02  X  FRE  @0 Virus dengue @2 NW @5 02
C03 02  X  ENG  @0 Dengue virus @2 NW @5 02
C03 02  X  SPA  @0 Dengue virus @2 NW @5 02
C03 03  X  FRE  @0 Animal @5 05
C03 03  X  ENG  @0 Animal @5 05
C03 03  X  SPA  @0 Animal @5 05
C03 04  X  FRE  @0 Anticorps monoclonal @5 06
C03 04  X  ENG  @0 Monoclonal antibody @5 06
C03 04  X  SPA  @0 Anticuerpo monoclonal @5 06
C03 05  X  FRE  @0 Sérotype @5 07
C03 05  X  ENG  @0 Serotype @5 07
C03 05  X  SPA  @0 Serotipo @5 07
C03 06  X  FRE  @0 Microbiologie @5 08
C03 06  X  ENG  @0 Microbiology @5 08
C03 06  X  SPA  @0 Microbiología @5 08
C07 01  X  FRE  @0 Rodentia @2 NS
C07 01  X  ENG  @0 Rodentia @2 NS
C07 01  X  SPA  @0 Rodentia @2 NS
C07 02  X  FRE  @0 Mammalia @2 NS
C07 02  X  ENG  @0 Mammalia @2 NS
C07 02  X  SPA  @0 Mammalia @2 NS
C07 03  X  FRE  @0 Vertebrata @2 NS
C07 03  X  ENG  @0 Vertebrata @2 NS
C07 03  X  SPA  @0 Vertebrata @2 NS
C07 04  X  FRE  @0 Virus groupe dengue @2 NW
C07 04  X  ENG  @0 Dengue group virus @2 NW
C07 04  X  SPA  @0 Dengue group virus @2 NW
C07 05  X  FRE  @0 Flavivirus @2 NW
C07 05  X  ENG  @0 Flavivirus @2 NW
C07 05  X  SPA  @0 Flavivirus @2 NW
C07 06  X  FRE  @0 Flaviviridae @2 NW
C07 06  X  ENG  @0 Flaviviridae @2 NW
C07 06  X  SPA  @0 Flaviviridae @2 NW
C07 07  X  FRE  @0 Virus @2 NW
C07 07  X  ENG  @0 Virus @2 NW
C07 07  X  SPA  @0 Virus @2 NW
N21       @1 117
N44 01      @1 OTO
N82       @1 OTO

Format Inist (serveur)

NO : PASCAL 09-0162365 INIST
ET : On a mouse monoclonal antibody that neutralizes all four dengue virus serotypes
AU : RAJAMANONMANI (Ravikumar); NKENFOU (Celine); CLANCY (Paula); YIN HOE YAU; GEIFMAN SHOCHAT (Susana); SUKUPOLVI-PETTY (Soila); SCHUL (Wouter); DIAMOND (Michael S.); VASUDEVAN (Subhash G.); LESCAR (Julien)
AF : School of Biological Sciences, Nanyang Technological University/Biopolis/Singapour (1 aut., 4 aut., 5 aut., 10 aut.); Program in Emerging Infectious Diseases, Duke-NUS, Graduate Medical School/Singapour (1 aut., 9 aut.); Novartis Institute for Tropical Diseases/Biopolis/Singapour (2 aut., 7 aut.); Department of Biochemistry and Molecular Biology, James Cook University/Australie (3 aut., 9 aut.); Departments of Medicine, Molecular Microbiology, Pathology and Immunology, Washington University School of Medicine/St Louis/Etats-Unis (6 aut., 8 aut.); AFMB CNRS UMR6098/Marseille/France (10 aut.)
DT : Publication en série; Niveau analytique
SO : Journal of general virology; ISSN 0022-1317; Coden JGVIAY; Royaume-Uni; Da. 2009; Vol. 90; No. p. 4; Pp. 799-809; Bibl. 1 p.3/4
LA : Anglais
EA : The flavivirus envelope glycoprotein (E) is responsible for viral attachment and entry by membrane fusion. Its ectodomain is the primary target of the humoral immune response. In particular, the C-terminal Ig-like domain III of E, which is exposed at the surface of the viral particle, forms an attractive antigen for raising protective monoclonal antibodies (mAb). 9F12, a mouse mAb raised against a dengue virus (DENV) serotype 2 recombinant domain III, cross-reacts with corresponding domains from the other three DENV serotypes and also with West Nile virus. mAb 9F1 2 binds with nanomolar affinity to a conserved epitope that maps to the viral surface comprising residues 305, 307, 310 and 330 of the E protein. mAb 9F1 2 neutralizes all four DENV serotypes in plaque reduction assays. We expressed a single-chain Fv from 9F12 that retains the binding activity of the parent mAb. Adsorption and fusion inhibition assays indicate that mAb 9F1 2 prevents early steps of viral entry. Its virus inhibition activity and broad cross-reactivity makes mAb 9F12 a suitable candidate for optimization and humanization into a therapeutic antibody to treat severe infections by dengue.
CC : 002A05C10; 002A05C07
FD : Souris; Virus dengue; Animal; Anticorps monoclonal; Sérotype; Microbiologie
FG : Rodentia; Mammalia; Vertebrata; Virus groupe dengue; Flavivirus; Flaviviridae; Virus
ED : Mouse; Dengue virus; Animal; Monoclonal antibody; Serotype; Microbiology
EG : Rodentia; Mammalia; Vertebrata; Dengue group virus; Flavivirus; Flaviviridae; Virus
SD : Ratón; Dengue virus; Animal; Anticuerpo monoclonal; Serotipo; Microbiología
LO : INIST-13533.354000187410180030
ID : 09-0162365

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Pascal:09-0162365

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<div type="abstract" xml:lang="en">The flavivirus envelope glycoprotein (E) is responsible for viral attachment and entry by membrane fusion. Its ectodomain is the primary target of the humoral immune response. In particular, the C-terminal Ig-like domain III of E, which is exposed at the surface of the viral particle, forms an attractive antigen for raising protective monoclonal antibodies (mAb). 9F12, a mouse mAb raised against a dengue virus (DENV) serotype 2 recombinant domain III, cross-reacts with corresponding domains from the other three DENV serotypes and also with West Nile virus. mAb 9F1 2 binds with nanomolar affinity to a conserved epitope that maps to the viral surface comprising residues 305, 307, 310 and 330 of the E protein. mAb 9F1 2 neutralizes all four DENV serotypes in plaque reduction assays. We expressed a single-chain Fv from 9F12 that retains the binding activity of the parent mAb. Adsorption and fusion inhibition assays indicate that mAb 9F1 2 prevents early steps of viral entry. Its virus inhibition activity and broad cross-reactivity makes mAb 9F12 a suitable candidate for optimization and humanization into a therapeutic antibody to treat severe infections by dengue.</div>
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<ET>On a mouse monoclonal antibody that neutralizes all four dengue virus serotypes</ET>
<AU>RAJAMANONMANI (Ravikumar); NKENFOU (Celine); CLANCY (Paula); YIN HOE YAU; GEIFMAN SHOCHAT (Susana); SUKUPOLVI-PETTY (Soila); SCHUL (Wouter); DIAMOND (Michael S.); VASUDEVAN (Subhash G.); LESCAR (Julien)</AU>
<AF>School of Biological Sciences, Nanyang Technological University/Biopolis/Singapour (1 aut., 4 aut., 5 aut., 10 aut.); Program in Emerging Infectious Diseases, Duke-NUS, Graduate Medical School/Singapour (1 aut., 9 aut.); Novartis Institute for Tropical Diseases/Biopolis/Singapour (2 aut., 7 aut.); Department of Biochemistry and Molecular Biology, James Cook University/Australie (3 aut., 9 aut.); Departments of Medicine, Molecular Microbiology, Pathology and Immunology, Washington University School of Medicine/St Louis/Etats-Unis (6 aut., 8 aut.); AFMB CNRS UMR6098/Marseille/France (10 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Journal of general virology; ISSN 0022-1317; Coden JGVIAY; Royaume-Uni; Da. 2009; Vol. 90; No. p. 4; Pp. 799-809; Bibl. 1 p.3/4</SO>
<LA>Anglais</LA>
<EA>The flavivirus envelope glycoprotein (E) is responsible for viral attachment and entry by membrane fusion. Its ectodomain is the primary target of the humoral immune response. In particular, the C-terminal Ig-like domain III of E, which is exposed at the surface of the viral particle, forms an attractive antigen for raising protective monoclonal antibodies (mAb). 9F12, a mouse mAb raised against a dengue virus (DENV) serotype 2 recombinant domain III, cross-reacts with corresponding domains from the other three DENV serotypes and also with West Nile virus. mAb 9F1 2 binds with nanomolar affinity to a conserved epitope that maps to the viral surface comprising residues 305, 307, 310 and 330 of the E protein. mAb 9F1 2 neutralizes all four DENV serotypes in plaque reduction assays. We expressed a single-chain Fv from 9F12 that retains the binding activity of the parent mAb. Adsorption and fusion inhibition assays indicate that mAb 9F1 2 prevents early steps of viral entry. Its virus inhibition activity and broad cross-reactivity makes mAb 9F12 a suitable candidate for optimization and humanization into a therapeutic antibody to treat severe infections by dengue.</EA>
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<FD>Souris; Virus dengue; Animal; Anticorps monoclonal; Sérotype; Microbiologie</FD>
<FG>Rodentia; Mammalia; Vertebrata; Virus groupe dengue; Flavivirus; Flaviviridae; Virus</FG>
<ED>Mouse; Dengue virus; Animal; Monoclonal antibody; Serotype; Microbiology</ED>
<EG>Rodentia; Mammalia; Vertebrata; Dengue group virus; Flavivirus; Flaviviridae; Virus</EG>
<SD>Ratón; Dengue virus; Animal; Anticuerpo monoclonal; Serotipo; Microbiología</SD>
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