Epitope mapping of neutralizing botulinum neurotoxin A antibodies by phage display

Infect Immun. 2001 Oct;69(10):6511-4. doi: 10.1128/IAI.69.10.6511-6514.2001.

Abstract

Single-chain antibodies neutralize activity and bind nonoverlapping epitopes of botulinum A neurotoxin. Two phage display epitope libraries were constructed from the 1.3 kb of binding domain cDNA. The minimal epitopes selected against the single-chain Fv-Fc antibodies correspond to conformational epitopes with amino acid residues 1115 to 1223 (S25), 1131 to 1264 (3D12), and 889 to 1294 (C25).

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Antibodies, Bacterial / immunology*
  • Botulinum Toxins, Type A / chemistry
  • Botulinum Toxins, Type A / genetics
  • Botulinum Toxins, Type A / immunology*
  • Clostridium botulinum / immunology*
  • Epitope Mapping / methods
  • Epitopes, B-Lymphocyte / chemistry
  • Epitopes, B-Lymphocyte / genetics
  • Epitopes, B-Lymphocyte / immunology*
  • Humans
  • Immunoglobulin Fragments / immunology*
  • Immunoglobulin Variable Region / immunology*
  • Mice
  • Models, Molecular
  • Neutralization Tests
  • Peptide Library
  • Protein Structure, Tertiary

Substances

  • Antibodies, Bacterial
  • Epitopes, B-Lymphocyte
  • Immunoglobulin Fragments
  • Immunoglobulin Variable Region
  • Peptide Library
  • immunoglobulin Fv
  • Botulinum Toxins, Type A