Inhibition of tetanus toxin fragment C binding to ganglioside G(T1b) by monoclonal antibodies recognizing different epitopes

Vaccine. 2000 Aug 15;19(1):114-21. doi: 10.1016/s0264-410x(00)00115-8.

Abstract

Anti-tetanus toxoid monoclonal antibodies would be useful in exploring the relationship of tetanus toxin structure to its function. Tetanus toxin fragment C has been shown to be responsible for binding to neurons via gangliosides. Eleven new and two previously derived monoclonal antibodies specific for tetanus toxin fragment C were shown to recognize five different fragment C epitopes, two of which were overlapping. Three of these epitopes participate in the binding to ganglioside G(T1b). One epitope was defined by a monoclonal antibody that did not inhibit the interaction between fragment C and ganglioside. This antibody however, was blocked from binding to fragment C by antibodies that were able to inhibit the fragment C-ganglioside interaction.

MeSH terms

  • Animals
  • Antibodies, Monoclonal / immunology*
  • Antibodies, Monoclonal / pharmacology
  • Binding, Competitive / drug effects
  • Cross Reactions
  • Epitopes, B-Lymphocyte / immunology
  • Female
  • Gangliosides / antagonists & inhibitors
  • Gangliosides / metabolism*
  • Mice
  • Mice, Inbred BALB C
  • Peptide Fragments / antagonists & inhibitors
  • Peptide Fragments / immunology
  • Peptide Fragments / metabolism*
  • Structure-Activity Relationship
  • Tetanus Toxin / antagonists & inhibitors
  • Tetanus Toxin / immunology
  • Tetanus Toxin / metabolism*

Substances

  • Antibodies, Monoclonal
  • Epitopes, B-Lymphocyte
  • Gangliosides
  • Peptide Fragments
  • Tetanus Toxin
  • tetanus toxin fragment C
  • trisialoganglioside GT1