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Related Experiment Videos

Shiga toxin: purification, structure, and function.

A Donohue-Rolfe1, D W Acheson, G T Keusch

  • 1Department of Medicine, New England Medical Center, Boston, Massachusetts 02111.

Reviews of Infectious Diseases
|March 1, 1991
PubMed
Summary

Shiga toxin, produced by Shigella dysenteriae, inhibits protein synthesis by damaging ribosomal RNA. Its structure includes an A chain for enzymatic activity and a B chain for cell binding, defining Shiga-like toxins.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Toxicology

Background:

  • Shiga toxin is a potent cytotoxin produced by Shigella dysenteriae type 1.
  • It exhibits cytotoxicity, enterotoxicity, and neurotoxicity, primarily by inhibiting protein synthesis.

Purpose of the Study:

  • To elucidate the structure-function relationship of Shiga toxin.
  • To understand the mechanism of protein synthesis inhibition and cell binding.

Main Methods:

  • Biochemical analysis of toxin structure and subunit function.
  • Identification of the specific rRNA target and cleavage site.

Main Results:

  • Shiga toxin comprises an A chain (32,225 Da) and a B chain (7,691 Da) in a 1:5 stoichiometry.

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  • The A chain cleaves adenine at nucleotide position 4324 in 28S rRNA, inhibiting protein synthesis.
  • The B chain facilitates toxin binding to cell surface receptors.

    • Conclusions:

    • Shiga toxin's mechanism involves specific rRNA cleavage by the A chain and receptor-mediated cell entry via the B chain.
    • This toxin serves as a prototype for structurally and functionally similar Shiga-like toxins.