Journal
MOVEMENT DISORDERS
Volume 19, Issue -, Pages S101-S108Publisher
WILEY
DOI: 10.1002/mds.20023
Keywords
monoclonal antibodies; toxin binding domain; potency; botulinum neurotoxin
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Funding
- NIAID NIH HHS [U01 AI056493, R21 AI53389-01] Funding Source: Medline
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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. (C) 2004 Movement Disorder Society.
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