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• W2808081722 abstract "Clostridium difficile is the major etiologic agent of antibiotic-associated intestinal disease. Pathogenesis of C. difficile is mainly attributed to the production and secretion of toxins A and B. Unlike most clostridial toxins, toxins A and B have no signal peptide, and they are therefore secreted by unusual mechanisms involving the holin-like TcdE protein and/or autolysis. In this study, we characterized the cell surface protein Cwp19, a newly identified peptidoglycan-degrading enzyme containing a novel catalytic domain. We purified a recombinant His6-tagged Cwp19 protein and showed that it has lytic transglycosylase activity. Moreover, we observed that Cwp19 is involved in cell autolysis and that a C. difficilecwp19 mutant exhibited delayed autolysis in stationary phase compared to the wild type when bacteria were grown in brain heart infusion (BHI) medium. Wild-type cell autolysis is correlated to strong alterations of cell wall thickness and integrity and to release of cytoplasmic material. Furthermore, we demonstrated that toxins were released into the extracellular medium as a result of Cwp19-induced autolysis when cells were grown in BHI medium. In contrast, Cwp19 did not induce autolysis or toxin release when cells were grown in tryptone-yeast extract (TY) medium. These data provide evidence for the first time that TcdE and bacteriolysis are coexisting mechanisms for toxin release, with their relative contributions in vitro depending on growth conditions. Thus, Cwp19 is an important surface protein involved in autolysis of vegetative cells of C. difficile that mediates the release of the toxins from the cell cytosol in response to specific environment conditions.IMPORTANCEClostridium difficile-associated disease is mainly known as a health care-associated infection. It represents the most problematic hospital-acquired infection in North America and Europe and exerts significant economic pressure on health care systems. Virulent strains of C. difficile generally produce two toxins that have been identified as the major virulence factors. The mechanism for release of these toxins from bacterial cells is not yet fully understood but is thought to be partly mediated by bacteriolysis. Here we identify a novel peptidoglycan hydrolase in C. difficile, Cwp19, exhibiting lytic transglycosylase activity. We show that Cwp19 contributes to C. difficile cell autolysis in the stationary phase and, consequently, to toxin release, most probably as a response to environmental conditions such as nutritional signals. These data highlight that Cwp19 constitutes a promising target for the development of new preventive and curative strategies." @default.
• W2808081722 created "2018-06-21" @default.
• W2808081722 creator A5009156340 @default.
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• W2808081722 date "2018-07-05" @default.
• W2808081722 modified "2023-10-04" @default.
• W2808081722 title "Cwp19 Is a Novel Lytic Transglycosylase Involved in Stationary-Phase Autolysis Resulting in Toxin Release in <i>Clostridium difficile</i>" @default.
• W2808081722 cites W1479743133 @default.
• W2808081722 cites W1509962568 @default.
• W2808081722 cites W1510123427 @default.
• W2808081722 cites W1518263193 @default.
• W2808081722 cites W1651660036 @default.
• W2808081722 cites W1809447830 @default.
• W2808081722 cites W1827851367 @default.
• W2808081722 cites W1856112995 @default.
• W2808081722 cites W1870791637 @default.
• W2808081722 cites W1911807020 @default.
• W2808081722 cites W1917165997 @default.
• W2808081722 cites W1928980316 @default.
• W2808081722 cites W1968718809 @default.
• W2808081722 cites W1984341893 @default.
• W2808081722 cites W1986270104 @default.
• W2808081722 cites W1994206535 @default.
• W2808081722 cites W2000755885 @default.
• W2808081722 cites W2001339596 @default.
• W2808081722 cites W2003466319 @default.
• W2808081722 cites W2008331309 @default.
• W2808081722 cites W2011299520 @default.
• W2808081722 cites W2012464397 @default.
• W2808081722 cites W2013726180 @default.
• W2808081722 cites W2015737379 @default.
• W2808081722 cites W2016794432 @default.
• W2808081722 cites W2018289835 @default.
• W2808081722 cites W2023464536 @default.
• W2808081722 cites W2025040342 @default.
• W2808081722 cites W2038231155 @default.
• W2808081722 cites W2040132528 @default.
• W2808081722 cites W2047204678 @default.
• W2808081722 cites W2047326410 @default.
• W2808081722 cites W2049812056 @default.
• W2808081722 cites W2050907729 @default.
• W2808081722 cites W2052779789 @default.
• W2808081722 cites W2053996120 @default.
• W2808081722 cites W2058127453 @default.
• W2808081722 cites W2058497286 @default.
• W2808081722 cites W2058983029 @default.
• W2808081722 cites W2061953031 @default.
• W2808081722 cites W2065851616 @default.
• W2808081722 cites W2065956804 @default.
• W2808081722 cites W2066394597 @default.
• W2808081722 cites W2067574120 @default.
• W2808081722 cites W2076701025 @default.
• W2808081722 cites W2090591880 @default.
• W2808081722 cites W2091521506 @default.
• W2808081722 cites W2093943421 @default.
• W2808081722 cites W2099047627 @default.
• W2808081722 cites W2099384916 @default.
• W2808081722 cites W2100092533 @default.
• W2808081722 cites W2100837269 @default.
• W2808081722 cites W2107277218 @default.
• W2808081722 cites W2110146873 @default.
• W2808081722 cites W2113998048 @default.
• W2808081722 cites W2115069651 @default.
• W2808081722 cites W2115499017 @default.
• W2808081722 cites W2129366833 @default.
• W2808081722 cites W2130696295 @default.
• W2808081722 cites W2131654062 @default.
• W2808081722 cites W2134091331 @default.
• W2808081722 cites W2135959117 @default.
• W2808081722 cites W2138447835 @default.
• W2808081722 cites W2141474738 @default.
• W2808081722 cites W2141885858 @default.
• W2808081722 cites W2144447845 @default.
• W2808081722 cites W2146333624 @default.
• W2808081722 cites W2147530224 @default.
• W2808081722 cites W2149941565 @default.
• W2808081722 cites W2151544157 @default.
• W2808081722 cites W2157129729 @default.
• W2808081722 cites W2158691001 @default.
• W2808081722 cites W2161268055 @default.
• W2808081722 cites W2163288778 @default.
• W2808081722 cites W2164424979 @default.
• W2808081722 cites W2166705194 @default.
• W2808081722 cites W2167703516 @default.
• W2808081722 cites W2168546011 @default.
• W2808081722 cites W2172070157 @default.
• W2808081722 cites W2192080449 @default.
• W2808081722 cites W2218002849 @default.
• W2808081722 cites W2293426014 @default.
• W2808081722 cites W2346369263 @default.

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