Cytosolic delivery and characterization of the TcdB glucosylating domain by using a heterologous protein fusion

Infect Immun. 2001 Jan;69(1):599-601. doi: 10.1128/IAI.69.1.599-601.2001.

Abstract

TcdB from Clostridium difficile glucosylates small GTPases (Rho, Rac, and Cdc42) and is an important virulence factor in the human disease pseudomembranous colitis. In these experiments, in-frame genetic fusions between the genes for the 255 amino-terminal residues of anthrax toxin lethal factor (LFn) and the TcdB(1-556) coding region were constructed, expressed, and purified from Escherichia coli. LFnTcdB(1-556) was enzymatically active and glucosylated recombinant RhoA, Rac, Cdc42, and substrates from cell extracts. LFnTcdB(1-556) plus anthrax toxin protective antigen intoxicated cultured mammalian cells and caused actin reorganization and mouse lethality, all similar to those caused by wild-type TcdB.

MeSH terms

  • Animals
  • Antigens, Bacterial*
  • Bacterial Toxins / isolation & purification
  • Bacterial Toxins / metabolism*
  • CHO Cells
  • Clostridioides difficile / pathogenicity*
  • Cricetinae
  • Cytosol / metabolism*
  • GTP Phosphohydrolases / metabolism
  • Glycosylation
  • Humans
  • Peptide Fragments / metabolism*
  • Recombinant Fusion Proteins / metabolism
  • Substrate Specificity

Substances

  • Antigens, Bacterial
  • Bacterial Toxins
  • Peptide Fragments
  • Recombinant Fusion Proteins
  • anthrax toxin
  • GTP Phosphohydrolases