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.
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Authors | L M Spyres, M Qa'Dan, A Meader, J J Tomasek, E W Howard, J D Ballard |
Journal | Infection and immunity
(Infect Immun)
Vol. 69
Issue 1
Pg. 599-601
(Jan 2001)
ISSN: 0019-9567 [Print] United States |
PMID | 11119561
(Publication Type: Journal Article)
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Chemical References |
- Antigens, Bacterial
- Bacterial Toxins
- Peptide Fragments
- Recombinant Fusion Proteins
- anthrax toxin
- GTP Phosphohydrolases
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Topics |
- Animals
- Antigens, Bacterial
- Bacterial Toxins
(isolation & purification, metabolism)
- CHO Cells
- Clostridioides difficile
(pathogenicity)
- Cricetinae
- Cytosol
(metabolism)
- GTP Phosphohydrolases
(metabolism)
- Glycosylation
- Humans
- Peptide Fragments
(metabolism)
- Recombinant Fusion Proteins
(metabolism)
- Substrate Specificity
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