Proceedings of the National Academy of Sciences · 2002 · 330 citations · 30 references
PharmacyImmunologyPharmaceutical BiotechnologyAntibody EngineeringImmunotherapyMonoclonal AntibodiesAntibody CharacterizationAntigen DesignBotulinum Toxin TherapyImmunoglobulin FunctionTherapeutic Monoclonal AntibodiesToxin-mediated DiseaseAntibody-mediated Toxin NeutralizationBotulinum NeurotoxinBotulinum ToxinsProtein Toxins
The botulinum neurotoxins (BoNTs) cause the paralytic human disease botulism and are one of the highest-risk threat agents for bioterrorism. To generate a pharmaceutical to prevent or treat botulism, monoclonal antibodies (mAbs) were generated by phage display and evaluated for neutralization of BoNT serotype A (BoNT/A) in vivo. Although no single mAb significantly neutralized toxin, a combination of three mAbs (oligoclonal Ab) neutralized 450,000 50% lethal doses of BoNT/A, a potency 90 times greater than human hyperimmune globulin. The potency of oligoclonal Ab was primarily due to a large increase in functional Ab binding affinity. The results indicate that the potency of the polyclonal humoral immune response can be deconvoluted to a few mAbs binding nonoverlapping epitopes, providing a route to drugs for preventing and treating botulism and diseases caused by other pathogens and biologic threat agents.
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Crystal structure of botulinum neurotoxin type A and implications for toxicity
D. Borden Lacy, William H. Tepp, A Cohen et al. · Nature Structural Biology · 1998 · 769 citations
Epitopes Involved in Antibody-Mediated Protection from Ebola Virus
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