NickelMaghrebV1, PascalFrancis, Corpus, bibRecord, 000179

Isolation and characterization of human neutralizing antibodies to rabies virus derived from a recombinant immune antibody library

Identifieur interne : 000179 ( PascalFrancis/Corpus ); précédent : 000178; suivant : 000180

Isolation and characterization of human neutralizing antibodies to rabies virus derived from a recombinant immune antibody library

Auteurs : Mehdi Houimel ; Koussay Dellagi

Source :

Journal of virological methods [ 0166-0934 ] ; 2009.

RBID : Pascal:09-0419589

Descripteurs français

Pascal (Inist)
- Homme, Virus rage, Isolement, Anticorps neutralisant, Virus recombinant, Technique phage display, Fragment peptidique Fab, Neutralisation, Microbiologie, Méthode.

English descriptors

KwdEn :
- Fab-Fragment, Human, Isolation, Method, Microbiology, Neutralization, Neutralizing antibody, Phage display, Rabies virus, Recombinant virus.

Abstract

A human immune Fab library was constructed using RNAs from peripheral blood lymphocytes obtained from rabies virus hyperimmune volunteers on phagemid vector. The size of the constructed Fab library was 2 x 10⁷ Escherichia coli transformants. After four rounds of panning on whole inactivated rabies virus (PV-11), phage clones displaying rabies virus-specific human Fab were selected. The specificity of soluble Fab antibody fragments, derived from positive phage clones was verified by ELISA. Among 20 specific Fab clones, the genetic sequence of 6 of them (FabRV01, FabRV02, FabRV03, FabRV04, FabRV05, and FabRV06) was analyzed. The variable heavy (VH) and variable light (VL) domains were found to share 90% and 93% homology with sequences encoded by the corresponding human germline genes, respectively. The soluble Fab fragments, expressed in Escherichia coli were purified by a single step Nickel-NTA affinity chromatography via a hexa-histidine tag and their binding specificities to rabies virus were confirmed. Three of the Fab antibodies, FabRV01, FabRV02 and FabRV03, showed binding characteristics to rabies virus glycoprotein antigenic site III with affinities in the K_D range 7 x 10^-9 to 5 × 10^-8 M. The Fab fragments showed dose-dependent neutralization properties for the challenge virus standard (CVS-11).

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

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A02	`01`			`@0 JVMEDH`
A03		`1`		`@0 J. virol. methods`
A05				`@2 161`
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A08	`01`	`1`	`ENG`	`@1 Isolation and characterization of human neutralizing antibodies to rabies virus derived from a recombinant immune antibody library`
A11	`01`	`1`		`@1 HOUIMEL (Mehdi)`
A11	`02`	`1`		`@1 DELLAGI (Koussay)`
A14	`01`			`@1 Laboratoire d'Immunopathologie Vaccinologie et Génétique Moléculaire, Institut Pasteur de Tunis @3 TUN @Z 1 aut. @Z 2 aut.`
A20				`@1 205-215`
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A23	`01`			`@0 ENG`
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A44				`@0 0000 @1 © 2009 INIST-CNRS. All rights reserved.`
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A60				`@1 P @3 PR`
A61				`@0 A`
A64	`01`	`1`		`@0 Journal of virological methods`
A66	`01`			`@0 NLD`
C01	`01`		`ENG`	@0 A human immune Fab library was constructed using RNAs from peripheral blood lymphocytes obtained from rabies virus hyperimmune volunteers on phagemid vector. The size of the constructed Fab library was 2 x 10⁷ Escherichia coli transformants. After four rounds of panning on whole inactivated rabies virus (PV-11), phage clones displaying rabies virus-specific human Fab were selected. The specificity of soluble Fab antibody fragments, derived from positive phage clones was verified by ELISA. Among 20 specific Fab clones, the genetic sequence of 6 of them (FabRV01, FabRV02, FabRV03, FabRV04, FabRV05, and FabRV06) was analyzed. The variable heavy (VH) and variable light (VL) domains were found to share 90% and 93% homology with sequences encoded by the corresponding human germline genes, respectively. The soluble Fab fragments, expressed in Escherichia coli were purified by a single step Nickel-NTA affinity chromatography via a hexa-histidine tag and their binding specificities to rabies virus were confirmed. Three of the Fab antibodies, FabRV01, FabRV02 and FabRV03, showed binding characteristics to rabies virus glycoprotein antigenic site III with affinities in the K_D range 7 x 10^-9 to 5 × 10^-8 M. The Fab fragments showed dose-dependent neutralization properties for the challenge virus standard (CVS-11).
C02	`01`	`X`		`@0 002A05C09`
C03	`01`	`X`	`FRE`	`@0 Homme @5 01`
C03	`01`	`X`	`ENG`	`@0 Human @5 01`
C03	`01`	`X`	`SPA`	`@0 Hombre @5 01`
C03	`02`	`X`	`FRE`	`@0 Virus rage @2 NW @5 02`
C03	`02`	`X`	`ENG`	`@0 Rabies virus @2 NW @5 02`
C03	`02`	`X`	`SPA`	`@0 Rabies virus @2 NW @5 02`
C03	`03`	`X`	`FRE`	`@0 Isolement @5 05`
C03	`03`	`X`	`ENG`	`@0 Isolation @5 05`
C03	`03`	`X`	`SPA`	`@0 Aislamiento @5 05`
C03	`04`	`X`	`FRE`	`@0 Anticorps neutralisant @5 06`
C03	`04`	`X`	`ENG`	`@0 Neutralizing antibody @5 06`
C03	`04`	`X`	`SPA`	`@0 anticuerpo neutralizante @5 06`
C03	`05`	`X`	`FRE`	`@0 Virus recombinant @5 07`
C03	`05`	`X`	`ENG`	`@0 Recombinant virus @5 07`
C03	`05`	`X`	`SPA`	`@0 Virus recombinante @5 07`
C03	`06`	`X`	`FRE`	`@0 Technique phage display @5 08`
C03	`06`	`X`	`ENG`	`@0 Phage display @5 08`
C03	`06`	`X`	`SPA`	`@0 Técnica phage display @5 08`
C03	`07`	`X`	`FRE`	`@0 Fragment peptidique Fab @5 09`
C03	`07`	`X`	`ENG`	`@0 Fab-Fragment @5 09`
C03	`07`	`X`	`SPA`	`@0 Fragmento peptídico Fab @5 09`
C03	`08`	`X`	`FRE`	`@0 Neutralisation @5 10`
C03	`08`	`X`	`ENG`	`@0 Neutralization @5 10`
C03	`08`	`X`	`SPA`	`@0 Neutralización @5 10`
C03	`09`	`X`	`FRE`	`@0 Microbiologie @5 11`
C03	`09`	`X`	`ENG`	`@0 Microbiology @5 11`
C03	`09`	`X`	`SPA`	`@0 Microbiología @5 11`
C03	`10`	`X`	`FRE`	`@0 Méthode @5 12`
C03	`10`	`X`	`ENG`	`@0 Method @5 12`
C03	`10`	`X`	`SPA`	`@0 Método @5 12`
C07	`01`	`X`	`FRE`	`@0 Lyssavirus @2 NW`
C07	`01`	`X`	`ENG`	`@0 Lyssavirus @2 NW`
C07	`01`	`X`	`SPA`	`@0 Lyssavirus @2 NW`
C07	`02`	`X`	`FRE`	`@0 Rhabdoviridae @2 NW`
C07	`02`	`X`	`ENG`	`@0 Rhabdoviridae @2 NW`
C07	`02`	`X`	`SPA`	`@0 Rhabdoviridae @2 NW`
C07	`03`	`X`	`FRE`	`@0 Mononegavirales @2 NW`
C07	`03`	`X`	`ENG`	`@0 Mononegavirales @2 NW`
C07	`03`	`X`	`SPA`	`@0 Mononegavirales @2 NW`
C07	`04`	`X`	`FRE`	`@0 Virus @2 NW`
C07	`04`	`X`	`ENG`	`@0 Virus @2 NW`
C07	`04`	`X`	`SPA`	`@0 Virus @2 NW`
N21				`@1 306`
N44	`01`			`@1 OTO`
N82				`@1 OTO`

Format Inist (serveur)

NO :	PASCAL 09-0419589 INIST
ET :	Isolation and characterization of human neutralizing antibodies to rabies virus derived from a recombinant immune antibody library
AU :	HOUIMEL (Mehdi); DELLAGI (Koussay)
AF :	Laboratoire d'Immunopathologie Vaccinologie et Génétique Moléculaire, Institut Pasteur de Tunis/Tunisie (1 aut., 2 aut.)
DT :	Publication en série; Papier de recherche; Niveau analytique
SO :	Journal of virological methods; ISSN 0166-0934; Coden JVMEDH; Pays-Bas; Da. 2009; Vol. 161; No. 2; Pp. 205-215; Bibl. 1 p.1/4
LA :	Anglais
EA :	A human immune Fab library was constructed using RNAs from peripheral blood lymphocytes obtained from rabies virus hyperimmune volunteers on phagemid vector. The size of the constructed Fab library was 2 x 10⁷ Escherichia coli transformants. After four rounds of panning on whole inactivated rabies virus (PV-11), phage clones displaying rabies virus-specific human Fab were selected. The specificity of soluble Fab antibody fragments, derived from positive phage clones was verified by ELISA. Among 20 specific Fab clones, the genetic sequence of 6 of them (FabRV01, FabRV02, FabRV03, FabRV04, FabRV05, and FabRV06) was analyzed. The variable heavy (VH) and variable light (VL) domains were found to share 90% and 93% homology with sequences encoded by the corresponding human germline genes, respectively. The soluble Fab fragments, expressed in Escherichia coli were purified by a single step Nickel-NTA affinity chromatography via a hexa-histidine tag and their binding specificities to rabies virus were confirmed. Three of the Fab antibodies, FabRV01, FabRV02 and FabRV03, showed binding characteristics to rabies virus glycoprotein antigenic site III with affinities in the K_D range 7 x 10^-9 to 5 × 10^-8 M. The Fab fragments showed dose-dependent neutralization properties for the challenge virus standard (CVS-11).
CC :	002A05C09
FD :	Homme; Virus rage; Isolement; Anticorps neutralisant; Virus recombinant; Technique phage display; Fragment peptidique Fab; Neutralisation; Microbiologie; Méthode
FG :	Lyssavirus; Rhabdoviridae; Mononegavirales; Virus
ED :	Human; Rabies virus; Isolation; Neutralizing antibody; Recombinant virus; Phage display; Fab-Fragment; Neutralization; Microbiology; Method
EG :	Lyssavirus; Rhabdoviridae; Mononegavirales; Virus
SD :	Hombre; Rabies virus; Aislamiento; anticuerpo neutralizante; Virus recombinante; Técnica phage display; Fragmento peptídico Fab; Neutralización; Microbiología; Método
LO :	INIST-18295.354000188113570040
ID :	09-0419589

Links to Exploration step

Pascal:09-0419589

Le document en format XML

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<front><div type="abstract" xml:lang="en">A human immune Fab library was constructed using RNAs from peripheral blood lymphocytes obtained from rabies virus hyperimmune volunteers on phagemid vector. The size of the constructed Fab library was 2 x 10<sup>7</sup>
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<fC01 i1="01" l="ENG"><s0>A human immune Fab library was constructed using RNAs from peripheral blood lymphocytes obtained from rabies virus hyperimmune volunteers on phagemid vector. The size of the constructed Fab library was 2 x 10<sup>7</sup>
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<server><NO>PASCAL 09-0419589 INIST</NO>
<ET>Isolation and characterization of human neutralizing antibodies to rabies virus derived from a recombinant immune antibody library</ET>
<AU>HOUIMEL (Mehdi); DELLAGI (Koussay)</AU>
<AF>Laboratoire d'Immunopathologie Vaccinologie et Génétique Moléculaire, Institut Pasteur de Tunis/Tunisie (1 aut., 2 aut.)</AF>
<DT>Publication en série; Papier de recherche; Niveau analytique</DT>
<SO>Journal of virological methods; ISSN 0166-0934; Coden JVMEDH; Pays-Bas; Da. 2009; Vol. 161; No. 2; Pp. 205-215; Bibl. 1 p.1/4</SO>
<LA>Anglais</LA>
<EA>A human immune Fab library was constructed using RNAs from peripheral blood lymphocytes obtained from rabies virus hyperimmune volunteers on phagemid vector. The size of the constructed Fab library was 2 x 10<sup>7</sup>
 Escherichia coli transformants. After four rounds of panning on whole inactivated rabies virus (PV-11), phage clones displaying rabies virus-specific human Fab were selected. The specificity of soluble Fab antibody fragments, derived from positive phage clones was verified by ELISA. Among 20 specific Fab clones, the genetic sequence of 6 of them (FabRV01, FabRV02, FabRV03, FabRV04, FabRV05, and FabRV06) was analyzed. The variable heavy (VH) and variable light (VL) domains were found to share 90% and 93% homology with sequences encoded by the corresponding human germline genes, respectively. The soluble Fab fragments, expressed in Escherichia coli were purified by a single step Nickel-NTA affinity chromatography via a hexa-histidine tag and their binding specificities to rabies virus were confirmed. Three of the Fab antibodies, FabRV01, FabRV02 and FabRV03, showed binding characteristics to rabies virus glycoprotein antigenic site III with affinities in the K<sub>D</sub>
 range 7 x 10<sup>-9</sup>
 to 5 × 10<sup>-8</sup>
 M. The Fab fragments showed dose-dependent neutralization properties for the challenge virus standard (CVS-11).</EA>
<CC>002A05C09</CC>
<FD>Homme; Virus rage; Isolement; Anticorps neutralisant; Virus recombinant; Technique phage display; Fragment peptidique Fab; Neutralisation; Microbiologie; Méthode</FD>
<FG>Lyssavirus; Rhabdoviridae; Mononegavirales; Virus</FG>
<ED>Human; Rabies virus; Isolation; Neutralizing antibody; Recombinant virus; Phage display; Fab-Fragment; Neutralization; Microbiology; Method</ED>
<EG>Lyssavirus; Rhabdoviridae; Mononegavirales; Virus</EG>
<SD>Hombre; Rabies virus; Aislamiento; anticuerpo neutralizante; Virus recombinante; Técnica phage display; Fragmento peptídico Fab; Neutralización; Microbiología; Método</SD>
<LO>INIST-18295.354000188113570040</LO>
<ID>09-0419589</ID>
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Isolation and characterization of human neutralizing antibodies to rabies virus derived from a recombinant immune antibody library

Isolation and characterization of human neutralizing antibodies to rabies virus derived from a recombinant immune antibody library

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