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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

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

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.[1]

References

  1. Cytosolic delivery and characterization of the TcdB glucosylating domain by using a heterologous protein fusion. Spyres, L.M., Qa'Dan, M., Meader, A., Tomasek, J.J., Howard, E.W., Ballard, J.D. Infect. Immun. (2001) [Pubmed]
 
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