On a mouse monoclonal antibody that neutralizes all four dengue virus serotypes
Identifieur interne : 002E89 ( PascalFrancis/Corpus ); précédent : 002E88; suivant : 002E90On 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 LescarSource :
- Journal of general virology [ 0022-1317 ] ; 2009.
Descripteurs français
- Pascal (Inist)
English descriptors
- KwdEn :
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.
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Pour connaître la documentation sur le format Inist Standard.
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Format Inist (serveur)
NO : | PASCAL 09-0162365 INIST |
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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:09-0162365Le document en format XML
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<front><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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<s2>NW</s2>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="SPA"><s0>Dengue virus</s0>
<s2>NW</s2>
<s5>02</s5>
</fC03>
<fC03 i1="03" i2="X" l="FRE"><s0>Animal</s0>
<s5>05</s5>
</fC03>
<fC03 i1="03" i2="X" l="ENG"><s0>Animal</s0>
<s5>05</s5>
</fC03>
<fC03 i1="03" i2="X" l="SPA"><s0>Animal</s0>
<s5>05</s5>
</fC03>
<fC03 i1="04" i2="X" l="FRE"><s0>Anticorps monoclonal</s0>
<s5>06</s5>
</fC03>
<fC03 i1="04" i2="X" l="ENG"><s0>Monoclonal antibody</s0>
<s5>06</s5>
</fC03>
<fC03 i1="04" i2="X" l="SPA"><s0>Anticuerpo monoclonal</s0>
<s5>06</s5>
</fC03>
<fC03 i1="05" i2="X" l="FRE"><s0>Sérotype</s0>
<s5>07</s5>
</fC03>
<fC03 i1="05" i2="X" l="ENG"><s0>Serotype</s0>
<s5>07</s5>
</fC03>
<fC03 i1="05" i2="X" l="SPA"><s0>Serotipo</s0>
<s5>07</s5>
</fC03>
<fC03 i1="06" i2="X" l="FRE"><s0>Microbiologie</s0>
<s5>08</s5>
</fC03>
<fC03 i1="06" i2="X" l="ENG"><s0>Microbiology</s0>
<s5>08</s5>
</fC03>
<fC03 i1="06" i2="X" l="SPA"><s0>Microbiología</s0>
<s5>08</s5>
</fC03>
<fC07 i1="01" i2="X" l="FRE"><s0>Rodentia</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>Rodentia</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="01" i2="X" l="SPA"><s0>Rodentia</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="02" i2="X" l="FRE"><s0>Mammalia</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="02" i2="X" l="ENG"><s0>Mammalia</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="02" i2="X" l="SPA"><s0>Mammalia</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="03" i2="X" l="FRE"><s0>Vertebrata</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="03" i2="X" l="ENG"><s0>Vertebrata</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="03" i2="X" l="SPA"><s0>Vertebrata</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="04" i2="X" l="FRE"><s0>Virus groupe dengue</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="04" i2="X" l="ENG"><s0>Dengue group virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="04" i2="X" l="SPA"><s0>Dengue group virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="05" i2="X" l="FRE"><s0>Flavivirus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="05" i2="X" l="ENG"><s0>Flavivirus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="05" i2="X" l="SPA"><s0>Flavivirus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="06" i2="X" l="FRE"><s0>Flaviviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="06" i2="X" l="ENG"><s0>Flaviviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="06" i2="X" l="SPA"><s0>Flaviviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="07" i2="X" l="FRE"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="07" i2="X" l="ENG"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="07" i2="X" l="SPA"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fN21><s1>117</s1>
</fN21>
<fN44 i1="01"><s1>OTO</s1>
</fN44>
<fN82><s1>OTO</s1>
</fN82>
</pA>
</standard>
<server><NO>PASCAL 09-0162365 INIST</NO>
<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>
<CC>002A05C10; 002A05C07</CC>
<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>
<LO>INIST-13533.354000187410180030</LO>
<ID>09-0162365</ID>
</server>
</inist>
</record>
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