High-affinity, protective antibodies to the binding domain of botulinum neurotoxin type A.

Journal Article (Journal Article)

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 H(C). Eleven neutralizing hybridomas were cloned, and their specific binding to BoNT/A H(C) was demonstrated by surface plasmon resonance, with dissociation constants ranging from 0.9 to <0.06 nM. Epitope mapping by real-time surface plasmon resonance showed that the antibodies bound to at least two distinct regions of the BoNT/A H(C) fragment. These MAbs will be useful tools for studying BoNT/A interactions with its receptor, and they have potential diagnostic and therapeutic applications.

Full Text

Duke Authors

Cited Authors

  • Pless, DD; Torres, ER; Reinke, EK; Bavari, S

Published Date

  • January 2001

Published In

Volume / Issue

  • 69 / 1

Start / End Page

  • 570 - 574

PubMed ID

  • 11119555

Pubmed Central ID

  • PMC97921

Electronic International Standard Serial Number (EISSN)

  • 1098-5522

International Standard Serial Number (ISSN)

  • 0019-9567

Digital Object Identifier (DOI)

  • 10.1128/iai.69.1.570-574.2001


  • eng