Chimerization and characterization of a monoclonal antibody with potent neutralizing activity across multiple influenza A H5N1 clades
Identifieur interne : 000079 ( PascalFrancis/Corpus ); précédent : 000078; suivant : 000080Chimerization and characterization of a monoclonal antibody with potent neutralizing activity across multiple influenza A H5N1 clades
Auteurs : Tze-Minn Mak ; Brendon J. Hanson ; Yee-Joo TanSource :
- Antiviral research [ 0166-3542 ] ; 2014.
Descripteurs français
- Pascal (Inist)
English descriptors
- KwdEn :
Abstract
The persistent evolution and circulation of highly pathogenic avian influenza H5N1 viruses pose a serious threat to global heath and hamper pandemic preparedness through conventional vaccine strategies. Combination passive immunotherapy using non-competing neutralizing antibodies has been proposed as a viable alternative to provide broad protection against drift variants. This necessitates the pre-pandemic production and characterization of potently neutralizing monoclonal antibodies (MAbs). One such antibody, MAb 9F4 was shown to provide heterologous protection against multiple H5N1 clade viruses, including one of the recently designated subclades, namely 2.3.4, through binding to a novel epitope, warranting its further development and characterization as a therapeutic candidate. In this study, the conversion of MAb 9F4 from mouse IgG2b to mouse-human chimeric (xi) IgG1 and IgA1 was achieved. These chimeric MAb versions were found to retain high degrees of binding and neutralizing activity against H5N1. The demonstration that xi-IgA1-9F4 retains a fairly high level of neutralizing activity, which is ˜10-fold lower than the corresponding xi-IgG1 isotype, suggests that this MAb could be further developed and engineered for intranasal administration.
Notice en format standard (ISO 2709)
Pour connaître la documentation sur le format Inist Standard.
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Format Inist (serveur)
NO : | PASCAL 14-0168547 INIST |
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ET : | Chimerization and characterization of a monoclonal antibody with potent neutralizing activity across multiple influenza A H5N1 clades |
AU : | MAK (Tze-Minn); HANSON (Brendon J.); TAN (Yee-Joo) |
AF : | NUS Graduate School for Integrative Sciences and Engineering, National University of Singapore/Singapour (1 aut.); Defence Medical and Environmental Research Institute, DSO National Laboratories/Singapour (2 aut.); Infrastructure, Technology and Translational Division, Institute of Molecular and Cell Biology, A*STAR/Singapour (3 aut.); Department of Microbiology, Yong Loo Lin School of Medicine, National University Health System (NUHS), National University of Singapore/Singapour (3 aut.) |
DT : | Publication en série; Niveau analytique |
SO : | Antiviral research; ISSN 0166-3542; Coden ARSRDR; Royaume-Uni; Da. 2014; Vol. 107; Pp. 76-83; Bibl. 1 p.1/4 |
LA : | Anglais |
EA : | The persistent evolution and circulation of highly pathogenic avian influenza H5N1 viruses pose a serious threat to global heath and hamper pandemic preparedness through conventional vaccine strategies. Combination passive immunotherapy using non-competing neutralizing antibodies has been proposed as a viable alternative to provide broad protection against drift variants. This necessitates the pre-pandemic production and characterization of potently neutralizing monoclonal antibodies (MAbs). One such antibody, MAb 9F4 was shown to provide heterologous protection against multiple H5N1 clade viruses, including one of the recently designated subclades, namely 2.3.4, through binding to a novel epitope, warranting its further development and characterization as a therapeutic candidate. In this study, the conversion of MAb 9F4 from mouse IgG2b to mouse-human chimeric (xi) IgG1 and IgA1 was achieved. These chimeric MAb versions were found to retain high degrees of binding and neutralizing activity against H5N1. The demonstration that xi-IgA1-9F4 retains a fairly high level of neutralizing activity, which is ˜10-fold lower than the corresponding xi-IgG1 isotype, suggests that this MAb could be further developed and engineered for intranasal administration. |
CC : | 002B02S05; 002B05C02C |
FD : | Caractérisation; Anticorps monoclonal; Multiple; Grippe; Anticorps neutralisant; Neutralisation; Hémagglutinine; Influenzavirus A(H5N1) |
FG : | Virose; Infection |
ED : | Characterization; Monoclonal antibody; Multiple; Influenza; Neutralizing antibody; Neutralization; Hemagglutinin; Influenzavirus A(H5N1) |
EG : | Viral disease; Infection |
SD : | Caracterización; Anticuerpo monoclonal; Múltiple; Gripe; anticuerpo neutralizante; Neutralización; Hemoaglutinina |
LO : | INIST-18839.354000502765430110 |
ID : | 14-0168547 |
Links to Exploration step
Pascal:14-0168547Le document en format XML
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<front><div type="abstract" xml:lang="en">The persistent evolution and circulation of highly pathogenic avian influenza H5N1 viruses pose a serious threat to global heath and hamper pandemic preparedness through conventional vaccine strategies. Combination passive immunotherapy using non-competing neutralizing antibodies has been proposed as a viable alternative to provide broad protection against drift variants. This necessitates the pre-pandemic production and characterization of potently neutralizing monoclonal antibodies (MAbs). One such antibody, MAb 9F4 was shown to provide heterologous protection against multiple H5N1 clade viruses, including one of the recently designated subclades, namely 2.3.4, through binding to a novel epitope, warranting its further development and characterization as a therapeutic candidate. In this study, the conversion of MAb 9F4 from mouse IgG<sub>2b</sub>
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<server><NO>PASCAL 14-0168547 INIST</NO>
<ET>Chimerization and characterization of a monoclonal antibody with potent neutralizing activity across multiple influenza A H5N1 clades</ET>
<AU>MAK (Tze-Minn); HANSON (Brendon J.); TAN (Yee-Joo)</AU>
<AF>NUS Graduate School for Integrative Sciences and Engineering, National University of Singapore/Singapour (1 aut.); Defence Medical and Environmental Research Institute, DSO National Laboratories/Singapour (2 aut.); Infrastructure, Technology and Translational Division, Institute of Molecular and Cell Biology, A*STAR/Singapour (3 aut.); Department of Microbiology, Yong Loo Lin School of Medicine, National University Health System (NUHS), National University of Singapore/Singapour (3 aut.)</AF>
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<EA>The persistent evolution and circulation of highly pathogenic avian influenza H5N1 viruses pose a serious threat to global heath and hamper pandemic preparedness through conventional vaccine strategies. Combination passive immunotherapy using non-competing neutralizing antibodies has been proposed as a viable alternative to provide broad protection against drift variants. This necessitates the pre-pandemic production and characterization of potently neutralizing monoclonal antibodies (MAbs). One such antibody, MAb 9F4 was shown to provide heterologous protection against multiple H5N1 clade viruses, including one of the recently designated subclades, namely 2.3.4, through binding to a novel epitope, warranting its further development and characterization as a therapeutic candidate. In this study, the conversion of MAb 9F4 from mouse IgG<sub>2b</sub>
to mouse-human chimeric (xi) IgG<sub>1</sub>
and IgA<sub>1</sub>
was achieved. These chimeric MAb versions were found to retain high degrees of binding and neutralizing activity against H5N1. The demonstration that xi-IgA<sub>1</sub>
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