High-Affinity, Protective Antibodies to the Binding Domain of Botulinum Neurotoxin Type A
Open Access
- 1 January 2001
- journal article
- Published by American Society for Microbiology in Infection and Immunity
- Vol. 69 (1) , 570-574
- https://doi.org/10.1128/iai.69.1.570-574.2001
Abstract
Monoclonal antibodies (MAbs) were prepared against the putative binding domain of botulinum neurotoxin A (BoNT/A), a nontoxic 50-kDa fragment. Initially, all fusion products were screened against the holotoxin BoNT/A and against the binding fragment, BoNT/A HC. Eleven neutralizing hybridomas were cloned, and their specific binding to BoNT/A HC was demonstrated by surface plasmon resonance, with dissociation constants ranging from 0.9 to C fragment. These MAbs will be useful tools for studying BoNT/A interactions with its receptor, and they have potential diagnostic and therapeutic applications.Keywords
This publication has 32 references indexed in Scilit:
- Sequence homology and structural analysis of the clostridial neurotoxinsJournal of Molecular Biology, 1999
- Unraveling the structures and modes of action of bacterial toxinsCurrent Opinion in Structural Biology, 1998
- Identifying the principal protective antigenic determinants of type A botulinum neurotoxinVaccine, 1998
- Crystal structure of botulinum neurotoxin type A and implications for toxicityNature Structural & Molecular Biology, 1998
- Structure of the receptor binding fragment HC of tetanus neurotoxinNature Structural & Molecular Biology, 1997
- Identification and Characterization of a Neutralizing Monoclonal Antibody Against Botulinum Neurotoxin, Serotype F, Following Vaccination With Active ToxinHybridoma, 1997
- Mapping of protective and cross-reactive domains of the type A neurotoxin of Clostridium botulinumVaccine, 1996
- Tetanus and Botulism NeurotoxinsPublished by Springer Nature ,1996
- Mechanism of action of tetanus and botulinum neurotoxinsMolecular Microbiology, 1994
- Botulinum neurotoxin A selectively cleaves the synaptic protein SNAP-25Nature, 1993