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Delineating the susceptibility of botulinum neurotoxins to denaturation through thermal effects

Academic Article
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Overview

authors

  • Zhou, Bin
  • Pellett, S.
  • Johnson, E. A.
  • Janda, Kim
  • Tepp, W. H.
  • Zhou, H.

publication date

  • April 2008

journal

  • FEBS Letters  Journal

abstract

  • Botulinum neurotoxins (BoNT) are the etiological agents responsible for botulism and are acknowledged terrorist threat agents. Passive immunotherapy may provide one countermeasure. Importantly, in the virtually unlimited repertoire of antibody specificities, enzyme linked immunosorbent assays (ELISA) has become an indispensable method for antibody selection. We report that of the BoNTs, BoNT/E is highly susceptible to polystyrene induced denaturation. To further dissect this result and the potential susceptibility of other BoNTs to denaturation we selected a thermal platform, which could be readily quantified using surface plasmon resonance (SPR), a primary rat spinal cord cell-based assay and an animal lethality model.

subject areas

  • Animals
  • Antibodies, Monoclonal
  • Biological Assay
  • Botulinum Toxins
  • Enzyme-Linked Immunosorbent Assay
  • Hot Temperature
  • Humans
  • Mice
  • Polystyrenes
  • Protein Conformation
  • Protein Denaturation
  • Rabbits
  • Rats
  • Surface Plasmon Resonance
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Research

keywords

  • antibody-toxin interaction
  • botulinum neurotoxin
  • surface plasmon resonance
  • toxin stability
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Identity

International Standard Serial Number (ISSN)

  • 0014-5793

Digital Object Identifier (DOI)

  • 10.1016/j.febslet.2008.03.047

PubMed ID

  • 18396167
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Additional Document Info

start page

  • 1526

end page

  • 1531

volume

  • 582

issue

  • 10

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