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Clostridioides difficile infection [5] (CDI or C-diff), also known as Clostridium difficile infection, is a symptomatic infection due to the spore-forming bacterium Clostridioides difficile. [6] Symptoms include watery diarrhea, fever, nausea, and abdominal pain. [1] It makes up about 20% of cases of antibiotic-associated diarrhea. [1]
The toxins function by damaging the intestinal mucosa and cause the symptoms of C. difficile infection, including pseudomembranous colitis. TcdA is one of the largest bacterial toxins known. With a molecular mass of 308 kDa, it is usually described as a potent enterotoxin , [ 3 ] but it also has some activity as a cytotoxin . [ 4 ]
Clostridioides difficile (syn. Clostridium difficile) is a bacterium known for causing serious diarrheal infections, and may also cause colon cancer. [4] [5] It is known also as C. difficile, or C. diff (/ s iː d ɪ f /), and is a Gram-positive species of spore-forming bacteria. [6]
Bezlotoxumab is a human monoclonal antibody designed for the prevention of recurrence of Clostridium difficile infections. By x-ray crystallized structure of N-terminal of TcdB, the toxin is identified to consist of three domains: a glucosyltransferase domain (GTD), a cysteine protease and a combined repetitive oligopeptide (CROP) domain.
Actoxumab is a human monoclonal antibody designed for the prevention of recurrence of Clostridioides difficile infection. [1]This drug, along with bezlotoxumab, was developed through Phase II efficacy trials by a partnership between Medarex Inc and MassBiologics of the University of Massachusetts Medical School. [2]
By x-ray crystallized structure of N-terminal of Clostridioides difficile toxin B (TcdB), the toxin was identified to consist of three domains: a GTD, a cysteine protease and a combined repetitive oligopeptides, CROP domain. The CROP domain consists of four different peptide units: B1, B2, B3, and B4.
Proteolytically processed clostridial cytotoxins A (306 kDa; TC# 1.C.57.1.2) and B (269 kDa; TC# 1.C.57.1.1) are O-glycosyltransferases that modify small GTPases of the Rho family by glucosylation of threonine residues, thereby blocking the action of the GTPases as switches of signal processes such as those mediated by the actin cytoskeleton.
Neutralizing antibodies on the other hand can neutralize the biological effects of the antigen without a need for immune cells. In some cases, non-neutralizing antibodies, or an insufficient amount of neutralizing antibodies binding to viral particles, can be utilized by some species of virus to facilitate uptake into their host cells.
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