Cell type and receptor identity regulate cholera toxin subunit B (CTB) internalization
نویسندگان
چکیده
منابع مشابه
Fusion of Cholera toxin B subunit (ctxB) with Shigella dysenteriae type I toxin B subunit (stxB), Cloning and Expression that in E. coli
Background and Objective: Shiga toxin (STx) is the main virulence factor in Shigella Dysenteriae type I and is composed of an enzymatic subunit STxA monomer and a receptor-binding STxB homopentamer. Shigella toxin B subunit (STxB) is a non-toxic homopentameric protein responsible for toxin binding and internalization into target cells by interacting with glycolipid (Gb3). Cholera toxi...
متن کاملSurface immobilized cholera toxin B subunit (CTB) facilitates vesicle docking, trafficking and exocytosis.
The subunit B of cholera toxin (CTB), which specifically binds with ganglioside GM1 enriched in membrane lipid rafts, is known to interfere with multiple cell functions. However, the specific, stable and spatially defined membrane signaling induced by CTB binding is often difficult to investigate by applying CTB molecules in bulk solution due to quick internalization, elicited intracellular rea...
متن کاملCholera toxin internalization and intoxication.
We read, with considerable dismay, a recent Research Article on cholera toxin (CT) internalization (Torgersen et al., 2001), in which the authors extensively challenged methods, results and conclusions that we had published four years ago (Orlandi and Fishman, 1998). As space limits a point-by-point rebuttal of their comments and critique of the many deficiencies in their study, we encourage re...
متن کاملproduction of pentameric cholera toxin b subunit in escherichia coli
cholera toxin b subunit (ctb) has been extensively studied as an immunogen, adjuvant, and inducer of oral tolerance in many investigations. production of ctb has been carried out in the bacterial, plant, insect and yeast expression systems. in this study the expression of the ctb containing a 6xhis-tagged was performed by escherichia coli (e.coli) m15. the yield of purified pentameric recombina...
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ژورنال
عنوان ژورنال: Interface Focus
سال: 2019
ISSN: 2042-8898,2042-8901
DOI: 10.1098/rsfs.2018.0076