Structure-Function Relationship of Botulinum and Tetanus Neurotoxins

  • Bal Ram Singh

Abstract

Botulinum and tetanus neurotoxins belong to a general group of bacterial protein toxins with a distinctive characteristics in terms of three structural domains with different complementary functions (Fig. 1). Other toxins of this group include cholera, diphtheria and Pseudomonas exotoxin A. These toxins have a polypeptide segment devoted to establish the binding with the target cell, apolypeptide segment that primarily helps translocate the whole or apart of the toxin across the cell membrane, and a third polypeptide segment which possesses an enzymatic or other putative biological activity capable of interfering with certain biochemical reactions within its target cells. Although the third domain elicits the ultimate toxic action, the other two domains are equally important for the biological action of the cellular toxicity of this group of toxins.

Keywords

Light Chain Heavy Chain Botulinum Toxin Membrane Channel Botulinum Neurotoxin 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1993

Authors and Affiliations

  • Bal Ram Singh
    • 1
  1. 1.Department of ChemistryUniversity of Massachusetts at DartmouthN. DartmouthUSA

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