Deciphering antibody properties that lead to potent botulinum neurotoxin neutralization.
Identifieur interne : 000D78 ( Ncbi/Merge ); précédent : 000D77; suivant : 000D79Deciphering antibody properties that lead to potent botulinum neurotoxin neutralization.
Auteurs : James D. Marks [États-Unis]Source :
- Movement disorders : official journal of the Movement Disorder Society [ 0885-3185 ] ; 2004.
English descriptors
- KwdEn :
- Animals, Antibodies, Monoclonal (immunology), Antibodies, Monoclonal (pharmacology), Antibody Specificity, Antigen-Antibody Reactions (physiology), Botulinum Toxins, Type A (immunology), Botulinum Toxins, Type A (pharmacology), Botulism (prevention & control), Dose-Response Relationship, Drug, Drug Synergism, Enzyme-Linked Immunosorbent Assay (methods), Epitope Mapping, Humans, Lethal Dose 50, Neuromuscular Agents (immunology), Neuromuscular Agents (pharmacology), Neurotoxins (metabolism), Neutralization Tests (methods).
- MESH :
- chemical , immunology : Antibodies, Monoclonal, Botulinum Toxins, Type A, Neuromuscular Agents.
- chemical , metabolism : Neurotoxins.
- chemical , pharmacology : Antibodies, Monoclonal, Botulinum Toxins, Type A, Neuromuscular Agents.
- methods : Enzyme-Linked Immunosorbent Assay, Neutralization Tests.
- physiology : Antigen-Antibody Reactions.
- prevention & control : Botulism.
- Animals, Antibody Specificity, Dose-Response Relationship, Drug, Drug Synergism, Epitope Mapping, Humans, Lethal Dose 50.
Abstract
Monoclonal antibodies (mAbs) have been developed that bind to the toxin binding domain (H(C)) of botulinum toxin type A. These mAbs recognize with high affinity nonoverlapping epitopes on native toxin. The potency of a combination of three of the mAbs is almost 100 times greater than that reported for human polyclonal botulinum immune globulin. Potency appears to result largely from a marked increase in binding affinity for toxin that results when antibodies are combined. Precise epitope, or even domain recognized, seems to be of much less importance. The very high affinity required for toxin neutralization suggests why single mAbs that potently neutralize toxin have not been reported. Such affinities are not typically generated by the immune response.
DOI: 10.1002/mds.20023
PubMed: 15027061
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pubmed:15027061Le document en format XML
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<term>Antibodies, Monoclonal (pharmacology)</term>
<term>Antibody Specificity</term>
<term>Antigen-Antibody Reactions (physiology)</term>
<term>Botulinum Toxins, Type A (immunology)</term>
<term>Botulinum Toxins, Type A (pharmacology)</term>
<term>Botulism (prevention & control)</term>
<term>Dose-Response Relationship, Drug</term>
<term>Drug Synergism</term>
<term>Enzyme-Linked Immunosorbent Assay (methods)</term>
<term>Epitope Mapping</term>
<term>Humans</term>
<term>Lethal Dose 50</term>
<term>Neuromuscular Agents (immunology)</term>
<term>Neuromuscular Agents (pharmacology)</term>
<term>Neurotoxins (metabolism)</term>
<term>Neutralization Tests (methods)</term>
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<term>Botulinum Toxins, Type A</term>
<term>Neuromuscular Agents</term>
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<term>Botulinum Toxins, Type A</term>
<term>Neuromuscular Agents</term>
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<keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Enzyme-Linked Immunosorbent Assay</term>
<term>Neutralization Tests</term>
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<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Antigen-Antibody Reactions</term>
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<keywords scheme="MESH" qualifier="prevention & control" xml:lang="en"><term>Botulism</term>
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<term>Antibody Specificity</term>
<term>Dose-Response Relationship, Drug</term>
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<front><div type="abstract" xml:lang="en">Monoclonal antibodies (mAbs) have been developed that bind to the toxin binding domain (H(C)) of botulinum toxin type A. These mAbs recognize with high affinity nonoverlapping epitopes on native toxin. The potency of a combination of three of the mAbs is almost 100 times greater than that reported for human polyclonal botulinum immune globulin. Potency appears to result largely from a marked increase in binding affinity for toxin that results when antibodies are combined. Precise epitope, or even domain recognized, seems to be of much less importance. The very high affinity required for toxin neutralization suggests why single mAbs that potently neutralize toxin have not been reported. Such affinities are not typically generated by the immune response.</div>
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<JournalIssue CitedMedium="Print"><Volume>19 Suppl 8</Volume>
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<Month>Mar</Month>
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<Title>Movement disorders : official journal of the Movement Disorder Society</Title>
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<Abstract><AbstractText>Monoclonal antibodies (mAbs) have been developed that bind to the toxin binding domain (H(C)) of botulinum toxin type A. These mAbs recognize with high affinity nonoverlapping epitopes on native toxin. The potency of a combination of three of the mAbs is almost 100 times greater than that reported for human polyclonal botulinum immune globulin. Potency appears to result largely from a marked increase in binding affinity for toxin that results when antibodies are combined. Precise epitope, or even domain recognized, seems to be of much less importance. The very high affinity required for toxin neutralization suggests why single mAbs that potently neutralize toxin have not been reported. Such affinities are not typically generated by the immune response.</AbstractText>
<CopyrightInformation>Copyright 2004 Movement Disorder Society</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Marks</LastName>
<ForeName>James D</ForeName>
<Initials>JD</Initials>
<AffiliationInfo><Affiliation>Department of Anesthesia and Pharmaceutical Chemistry, University of California, San Francisco General Hospital, San Francisco, California 94110, USA. marksj@anesthesia.ucsf.edu</Affiliation>
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<Language>eng</Language>
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