Detection of antibodies against botulinum toxins
Identifieur interne :
000A75 ( PascalFrancis/Curation );
précédent :
000A74;
suivant :
000A76
Detection of antibodies against botulinum toxins
Auteurs : Dorothea Sesardic [
Royaume-Uni] ;
Russell G. A. Jones [
Royaume-Uni] ;
Tong Leung [
Royaume-Uni] ;
Toni Alsop [
Royaume-Uni] ;
Robert Tierney [
Royaume-Uni]
Source :
-
Movement disorders [ 0885-3185 ] ; 2004.
RBID : Pascal:04-0228587
Descripteurs français
English descriptors
Abstract
After immunisation with botulinum vaccine, antibodies to multiple epitopes are produced. Only some of these will have the capacity to neutralise the toxin activity. In fact, the ability of toxoid vaccine to induce toxin neutralising antibodies has provided the basis for the use of therapeutic antitoxins and immunoglobulins for the prophylaxis and treatment of diseases caused by bacterial toxins. Increasing indications for the chronic use of botulinum toxin for therapy have inevitably resulted in concern for patients becoming unresponsive because of the presence of circulating toxin-specific antibodies. Highly sensitive and relevant assays to detect only clinically relevant toxin neutralising antibodies are essential. Although immunoassays often provide the sensitivity, their relevance and specificity is often questioned. The mouse protection LD50 bioassay is considered most relevant but can often only detect 10 mIU/ml of antitoxin. This sensitivity, although sufficient for confirming protective immunity, is inadequate for patients undergoing toxin therapy. An intramuscular paralysis assay improves the sensitivity to ca. 1 mIU/ml, and a mouse ex vivo diaphragm assay, with sensitivity of <0.5 mIU/ml, is the most sensitive functional assay to date for this purpose. Alternative approaches for the detection of antibodies to botulinum toxin have included in vitro endopeptidase activity neutralisation. Unlike any other functional assay, this approach is not reliant on serotype-specific antibodies for specificity. Most recent promising developments are focused on cellular assays utilising primary rat embryonic cord cells or more conveniently in vitro differentiated established cell lines such as human neuroblastoma cells.
pA |
A01 | 01 | 1 | | @0 0885-3185 |
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A03 | | 1 | | @0 Mov. disord. |
---|
A05 | | | | @2 19 |
---|
A06 | | | | @3 SUP8 |
---|
A08 | 01 | 1 | ENG | @1 Detection of antibodies against botulinum toxins |
---|
A09 | 01 | 1 | ENG | @1 Basic and Therapeutic Aspects of Neurotoxins |
---|
A11 | 01 | 1 | | @1 SESARDIC (Dorothea) |
---|
A11 | 02 | 1 | | @1 JONES (Russell G. A.) |
---|
A11 | 03 | 1 | | @1 LEUNG (Tong) |
---|
A11 | 04 | 1 | | @1 ALSOP (Toni) |
---|
A11 | 05 | 1 | | @1 TIERNEY (Robert) |
---|
A12 | 01 | 1 | | @1 BIGALKE (HANS) @9 ed. |
---|
A12 | 02 | 1 | | @1 DRESSLER (Dirk) @9 ed. |
---|
A12 | 03 | 1 | | @1 JANKOVIC (Joseph) @9 ed. |
---|
A14 | 01 | | | @1 Division of Bacteriology, National Institute for Biological Standards and Control @2 Potters Bar, Hertfordshire @3 GBR @Z 1 aut. @Z 2 aut. @Z 3 aut. @Z 4 aut. @Z 5 aut. |
---|
A15 | 01 | | | @1 Institute of Toxicology, Medical School of Hannover @2 Hannover @3 DEU @Z 1 aut. |
---|
A15 | 02 | | | @1 Department of Neurology, Rostock University @2 Rostock @3 DEU @Z 2 aut. |
---|
A15 | 03 | | | @1 Parkinson's Disease Center and Movement Disorders Clinic, Department of Neurology, Baylor College of Medicine @2 Houston, Texas @3 USA @Z 3 aut. |
---|
A20 | | | | @1 85-91 |
---|
A21 | | | | @1 2004 |
---|
A23 | 01 | | | @0 ENG |
---|
A43 | 01 | | | @1 INIST @2 20953 @5 354000113591720120 |
---|
A44 | | | | @0 0000 @1 © 2004 INIST-CNRS. All rights reserved. |
---|
A45 | | | | @0 66 ref. |
---|
A47 | 01 | 1 | | @0 04-0228587 |
---|
A60 | | | | @1 P @2 C |
---|
A61 | | | | @0 A |
---|
A64 | 01 | 1 | | @0 Movement disorders |
---|
A66 | 01 | | | @0 USA |
---|
C01 | 01 | | ENG | @0 After immunisation with botulinum vaccine, antibodies to multiple epitopes are produced. Only some of these will have the capacity to neutralise the toxin activity. In fact, the ability of toxoid vaccine to induce toxin neutralising antibodies has provided the basis for the use of therapeutic antitoxins and immunoglobulins for the prophylaxis and treatment of diseases caused by bacterial toxins. Increasing indications for the chronic use of botulinum toxin for therapy have inevitably resulted in concern for patients becoming unresponsive because of the presence of circulating toxin-specific antibodies. Highly sensitive and relevant assays to detect only clinically relevant toxin neutralising antibodies are essential. Although immunoassays often provide the sensitivity, their relevance and specificity is often questioned. The mouse protection LD50 bioassay is considered most relevant but can often only detect 10 mIU/ml of antitoxin. This sensitivity, although sufficient for confirming protective immunity, is inadequate for patients undergoing toxin therapy. An intramuscular paralysis assay improves the sensitivity to ca. 1 mIU/ml, and a mouse ex vivo diaphragm assay, with sensitivity of <0.5 mIU/ml, is the most sensitive functional assay to date for this purpose. Alternative approaches for the detection of antibodies to botulinum toxin have included in vitro endopeptidase activity neutralisation. Unlike any other functional assay, this approach is not reliant on serotype-specific antibodies for specificity. Most recent promising developments are focused on cellular assays utilising primary rat embryonic cord cells or more conveniently in vitro differentiated established cell lines such as human neuroblastoma cells. |
---|
C02 | 01 | X | | @0 002B17 |
---|
C03 | 01 | X | FRE | @0 Système nerveux pathologie @5 01 |
---|
C03 | 01 | X | ENG | @0 Nervous system diseases @5 01 |
---|
C03 | 01 | X | SPA | @0 Sistema nervioso patología @5 01 |
---|
C03 | 02 | X | FRE | @0 Dépistage @5 02 |
---|
C03 | 02 | X | ENG | @0 Medical screening @5 02 |
---|
C03 | 02 | X | SPA | @0 Descubrimiento @5 02 |
---|
C03 | 03 | X | FRE | @0 Bontoxilysin @2 FE @2 FR @5 03 |
---|
C03 | 03 | X | ENG | @0 Bontoxilysin @2 FE @2 FR @5 03 |
---|
C03 | 03 | X | SPA | @0 Bontoxilysin @2 FE @2 FR @5 03 |
---|
C07 | 01 | X | FRE | @0 Metalloendopeptidases @2 FE |
---|
C07 | 01 | X | ENG | @0 Metalloendopeptidases @2 FE |
---|
C07 | 01 | X | SPA | @0 Metalloendopeptidases @2 FE |
---|
C07 | 02 | X | FRE | @0 Peptidases @2 FE |
---|
C07 | 02 | X | ENG | @0 Peptidases @2 FE |
---|
C07 | 02 | X | SPA | @0 Peptidases @2 FE |
---|
C07 | 03 | X | FRE | @0 Hydrolases @2 FE |
---|
C07 | 03 | X | ENG | @0 Hydrolases @2 FE |
---|
C07 | 03 | X | SPA | @0 Hydrolases @2 FE |
---|
C07 | 04 | X | FRE | @0 Enzyme @2 FE |
---|
C07 | 04 | X | ENG | @0 Enzyme @2 FE |
---|
C07 | 04 | X | SPA | @0 Enzima @2 FE |
---|
N21 | | | | @1 145 |
---|
N82 | | | | @1 OTO |
---|
|
pR |
A30 | 01 | 1 | ENG | @1 Toxins 2002. Conference @3 Hannover DEU @4 2002 |
---|
|
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Le document en format XML
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<sZ>2 aut.</sZ>
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<author><name sortKey="Jones, Russell G A" sort="Jones, Russell G A" uniqKey="Jones R" first="Russell G. A." last="Jones">Russell G. A. Jones</name>
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<s2>Potters Bar, Hertfordshire</s2>
<s3>GBR</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
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<country>Royaume-Uni</country>
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<author><name sortKey="Leung, Tong" sort="Leung, Tong" uniqKey="Leung T" first="Tong" last="Leung">Tong Leung</name>
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<s2>Potters Bar, Hertfordshire</s2>
<s3>GBR</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
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<author><name sortKey="Alsop, Toni" sort="Alsop, Toni" uniqKey="Alsop T" first="Toni" last="Alsop">Toni Alsop</name>
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<s3>GBR</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
</inist:fA14>
<country>Royaume-Uni</country>
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<author><name sortKey="Tierney, Robert" sort="Tierney, Robert" uniqKey="Tierney R" first="Robert" last="Tierney">Robert Tierney</name>
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<sZ>2 aut.</sZ>
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<sZ>5 aut.</sZ>
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<country>Royaume-Uni</country>
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<front><div type="abstract" xml:lang="en">After immunisation with botulinum vaccine, antibodies to multiple epitopes are produced. Only some of these will have the capacity to neutralise the toxin activity. In fact, the ability of toxoid vaccine to induce toxin neutralising antibodies has provided the basis for the use of therapeutic antitoxins and immunoglobulins for the prophylaxis and treatment of diseases caused by bacterial toxins. Increasing indications for the chronic use of botulinum toxin for therapy have inevitably resulted in concern for patients becoming unresponsive because of the presence of circulating toxin-specific antibodies. Highly sensitive and relevant assays to detect only clinically relevant toxin neutralising antibodies are essential. Although immunoassays often provide the sensitivity, their relevance and specificity is often questioned. The mouse protection LD<sub>50</sub>
bioassay is considered most relevant but can often only detect 10 mIU/ml of antitoxin. This sensitivity, although sufficient for confirming protective immunity, is inadequate for patients undergoing toxin therapy. An intramuscular paralysis assay improves the sensitivity to ca. 1 mIU/ml, and a mouse ex vivo diaphragm assay, with sensitivity of <0.5 mIU/ml, is the most sensitive functional assay to date for this purpose. Alternative approaches for the detection of antibodies to botulinum toxin have included in vitro endopeptidase activity neutralisation. Unlike any other functional assay, this approach is not reliant on serotype-specific antibodies for specificity. Most recent promising developments are focused on cellular assays utilising primary rat embryonic cord cells or more conveniently in vitro differentiated established cell lines such as human neuroblastoma cells.</div>
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<fA08 i1="01" i2="1" l="ENG"><s1>Detection of antibodies against botulinum toxins</s1>
</fA08>
<fA09 i1="01" i2="1" l="ENG"><s1>Basic and Therapeutic Aspects of Neurotoxins</s1>
</fA09>
<fA11 i1="01" i2="1"><s1>SESARDIC (Dorothea)</s1>
</fA11>
<fA11 i1="02" i2="1"><s1>JONES (Russell G. A.)</s1>
</fA11>
<fA11 i1="03" i2="1"><s1>LEUNG (Tong)</s1>
</fA11>
<fA11 i1="04" i2="1"><s1>ALSOP (Toni)</s1>
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<fA11 i1="05" i2="1"><s1>TIERNEY (Robert)</s1>
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<fA12 i1="01" i2="1"><s1>BIGALKE (HANS)</s1>
<s9>ed.</s9>
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<fA12 i1="02" i2="1"><s1>DRESSLER (Dirk)</s1>
<s9>ed.</s9>
</fA12>
<fA12 i1="03" i2="1"><s1>JANKOVIC (Joseph)</s1>
<s9>ed.</s9>
</fA12>
<fA14 i1="01"><s1>Division of Bacteriology, National Institute for Biological Standards and Control</s1>
<s2>Potters Bar, Hertfordshire</s2>
<s3>GBR</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
</fA14>
<fA15 i1="01"><s1>Institute of Toxicology, Medical School of Hannover</s1>
<s2>Hannover</s2>
<s3>DEU</s3>
<sZ>1 aut.</sZ>
</fA15>
<fA15 i1="02"><s1>Department of Neurology, Rostock University</s1>
<s2>Rostock</s2>
<s3>DEU</s3>
<sZ>2 aut.</sZ>
</fA15>
<fA15 i1="03"><s1>Parkinson's Disease Center and Movement Disorders Clinic, Department of Neurology, Baylor College of Medicine</s1>
<s2>Houston, Texas</s2>
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<sZ>3 aut.</sZ>
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<fA20><s1>85-91</s1>
</fA20>
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<s5>354000113591720120</s5>
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<fA44><s0>0000</s0>
<s1>© 2004 INIST-CNRS. All rights reserved.</s1>
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<fA45><s0>66 ref.</s0>
</fA45>
<fA47 i1="01" i2="1"><s0>04-0228587</s0>
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<fA60><s1>P</s1>
<s2>C</s2>
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</fA66>
<fC01 i1="01" l="ENG"><s0>After immunisation with botulinum vaccine, antibodies to multiple epitopes are produced. Only some of these will have the capacity to neutralise the toxin activity. In fact, the ability of toxoid vaccine to induce toxin neutralising antibodies has provided the basis for the use of therapeutic antitoxins and immunoglobulins for the prophylaxis and treatment of diseases caused by bacterial toxins. Increasing indications for the chronic use of botulinum toxin for therapy have inevitably resulted in concern for patients becoming unresponsive because of the presence of circulating toxin-specific antibodies. Highly sensitive and relevant assays to detect only clinically relevant toxin neutralising antibodies are essential. Although immunoassays often provide the sensitivity, their relevance and specificity is often questioned. The mouse protection LD<sub>50</sub>
bioassay is considered most relevant but can often only detect 10 mIU/ml of antitoxin. This sensitivity, although sufficient for confirming protective immunity, is inadequate for patients undergoing toxin therapy. An intramuscular paralysis assay improves the sensitivity to ca. 1 mIU/ml, and a mouse ex vivo diaphragm assay, with sensitivity of <0.5 mIU/ml, is the most sensitive functional assay to date for this purpose. Alternative approaches for the detection of antibodies to botulinum toxin have included in vitro endopeptidase activity neutralisation. Unlike any other functional assay, this approach is not reliant on serotype-specific antibodies for specificity. Most recent promising developments are focused on cellular assays utilising primary rat embryonic cord cells or more conveniently in vitro differentiated established cell lines such as human neuroblastoma cells.</s0>
</fC01>
<fC02 i1="01" i2="X"><s0>002B17</s0>
</fC02>
<fC03 i1="01" i2="X" l="FRE"><s0>Système nerveux pathologie</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="ENG"><s0>Nervous system diseases</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="SPA"><s0>Sistema nervioso patología</s0>
<s5>01</s5>
</fC03>
<fC03 i1="02" i2="X" l="FRE"><s0>Dépistage</s0>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="ENG"><s0>Medical screening</s0>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="SPA"><s0>Descubrimiento</s0>
<s5>02</s5>
</fC03>
<fC03 i1="03" i2="X" l="FRE"><s0>Bontoxilysin</s0>
<s2>FE</s2>
<s2>FR</s2>
<s5>03</s5>
</fC03>
<fC03 i1="03" i2="X" l="ENG"><s0>Bontoxilysin</s0>
<s2>FE</s2>
<s2>FR</s2>
<s5>03</s5>
</fC03>
<fC03 i1="03" i2="X" l="SPA"><s0>Bontoxilysin</s0>
<s2>FE</s2>
<s2>FR</s2>
<s5>03</s5>
</fC03>
<fC07 i1="01" i2="X" l="FRE"><s0>Metalloendopeptidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>Metalloendopeptidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="01" i2="X" l="SPA"><s0>Metalloendopeptidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="FRE"><s0>Peptidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="ENG"><s0>Peptidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="SPA"><s0>Peptidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="03" i2="X" l="FRE"><s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="03" i2="X" l="ENG"><s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="03" i2="X" l="SPA"><s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="04" i2="X" l="FRE"><s0>Enzyme</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="04" i2="X" l="ENG"><s0>Enzyme</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="04" i2="X" l="SPA"><s0>Enzima</s0>
<s2>FE</s2>
</fC07>
<fN21><s1>145</s1>
</fN21>
<fN82><s1>OTO</s1>
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<pR><fA30 i1="01" i2="1" l="ENG"><s1>Toxins 2002. Conference</s1>
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