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- W3176771330 abstract "Clostridium difficile is an anaerobic, gram-positive bacterium and a common gastrointestinal pathogen. Two virulence factors of C. difficile known to mediate disease are Toxin A (TcdA) and Toxin B (TcdB). These toxins are glucosyltransferase-containing multi-domain proteins that enter the host's epithelial cells by binding to cell–surface carbohydrate antigens. Once inside the cell, the toxins undergo a pH-induced conformational change and release their glucosyltransferase domains (GTD), leading to disruption of cell cytoskeleton integrity. Existing treatments for C. difficile such as fecal transplants and antibiotics have not proven highly effective. Passive immunotherapy with inhibitory antibodies recognizing TcdA and TcdB is a promising alternative. Recombinant Camelidae antibodies (VHHs) that neutralize the toxins' function have been identified. TcdA's receptor-binding domain has seven repetitive elements known to interact with cell-surface carbohydrates. The VHH antibodies A20.1 and A26.8, which are known to neutralize TcdA, do not block the carbohydrate-binding site on TcdA directly, suggesting a novel mode of TcdA inhibition. The Ashbury College MSOE Center for BioMolecular Modeling SMART Team used 3-D modelling and printing technology to examine the structure-function relationships of a TcdA fragment (TcdA-A2) simultaneously bound to A20.1 and A26.8. The structure shows that the VHHs target distinct epitopes on the toxin and neutralize TcdA by a novel mechanism independent of the carbohydrate binding sites, providing a rationale for designing highly potent biparatopic TcdA-neutralizing antibodies. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal." @default.
- W3176771330 created "2021-07-05" @default.
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- W3176771330 date "2018-04-01" @default.
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- W3176771330 title "The Use of Single‐Domain Antibodies from Camelidae for the Inhibition of Clostridium difficile Toxins A and B" @default.
- W3176771330 doi "https://doi.org/10.1096/fasebj.2018.32.1_supplement.lb202" @default.
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