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• W1992294788 abstract "The neurotoxins from Clostridium botulinum (BoNT serotypes A-G) exert their lethal effect by preventing the release of acetylcholine at the neuromuscular junction. As with tetanus toxin, immunization with a non-toxic fragment, the 50 kDa C-terminal portion of BoNTA (HC; residues 861–1296), protects mice against lethal challenges with the intact toxin. To locate the neutralizing epitopes, several protective monoclonal antibodies (mAbs) against BoNTA-HC were isolated and cloned. Specific binding of the mAbs to BoNTA-HC was demonstrated by surface plasmon resonance, with Kds in the range of 10−10 to 10−11 M. These antibodies recognized a genetically engineered polypeptide (1150–1289) that was previously shown to induce protective immunity. Prior to the determination of the X-ray crystal structure of the tetanus neurotoxin HC fragment, molecular modelling studies indicated that it contained two highly solvent-exposed loops. Based on these predictions, two 25-mer HC-peptides corresponding to these two regions were synthesized and were demonstrated to bind the neutralizing mAbs. Mice immunized with the HC-peptides had high levels of antibodies that recognized BoNTA-HC. However, immunizations with only one of the HC peptides protected when mice were challenged with BoNTA. On the basis of these analyses, it should be possible to develop small peptides that could be useful in the design of future vaccines against these neurotoxins." @default.
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• W1992294788 date "1998-11-01" @default.
• W1992294788 modified "2023-10-10" @default.
• W1992294788 title "Identifying the principal protective antigenic determinants of type A botulinum neurotoxin" @default.
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• W1992294788 doi "https://doi.org/10.1016/s0264-410x(98)00175-3" @default.
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